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148 results on '"Burnett, Roger M."'

3. Insights into assembly from structural analysis of bacteriophage PRD1

Author

Abrescia, Nicola G. A., Cockburn, Joseph J. B., Grimes, Jonathan M., Sutton, Geoffrey C., Diprose, Jonathan M., Butcher, Sarah J., Fuller, Stephen D., San Martin, Carmen, Burnett, Roger M., Stuart, David I., Bamford, Dennis H., and Bamford, Jaana K. H.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Nicola G. A. Abrescia [1, 5]; Joseph J. B. Cockburn [1, 2, 5]; Jonathan M. Grimes [1]; Geoffrey C. Sutton [1]; Jonathan M. Diprose [1]; Sarah J. Butcher [3]; [...]

Published
2004
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4. The Bacillus thuringiensis linear double-stranded DNA phage Bam35, which is highly similar to the Bacillus cereus linear plasmid pBClin15, has a prophage state

Author

Stromsten, Nelli J., Benson, Stacy D., Burnett, Roger M., Bamford, Dennis H., and Bamford, Jaana K.H.

Subjects
Bacillus cereus -- Genetic aspects, Bacillus cereus -- Physiological aspects, Bacillus thuringiensis -- Genetic aspects, Bacillus thuringiensis -- Physiological aspects, Bacteriology -- Research, Bacteriophages -- Genetic aspects, Bacteriophages -- Physiological aspects, DNA -- Genetic aspects, Microbial populations -- Genetic aspects, Plasmids -- Genetic aspects, Plasmids -- Physiological aspects, Biological sciences
Abstract

Bam35, a 15-kbp double-stranded DNA phage, infects Bacillus thuringiensis. Recently, sequencing of the related Bacillus cereus revealed a 15.1-kbp linear plasmid, pBClin15. We show that pBClin15 closely resembles Bam35 and demonstrate conversion of Bam35 to a prophage. This state is common, as several B. thuringiensis strains release Bam35-related viruses.

Published
2003

6. Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures

Author

Benson, Stacy D., Bamford Jaana K.H., Bamford, Dennis H., and Burnett, Roger M.

Subjects
Viruses -- Evolution, Bacteriophages -- Genetic aspects, Adenoviruses, Human -- Research, Evolution -- Genetic aspects, Biological sciences
Abstract

Viral evolution as revealed by human adenovirus coat protein structures and bacteriophage PRD1 is discussed. The unusual PRD1 has a membrane beneath the outer icosahedral protein coat. Each of three interlocking subunits in the major coat protein has two 8-stranded viral jelly rolls that are normal for the viral capsid. The P3 molecule, which is the major coat protein, is much like hexon, the equivalent in human adenovirus. The striking similarities strongly suggest evolutionary relationship.

Published
1999

12. Structure of the Adenovirus Virion

Author

Burnett, Roger M., primary, Athappilly, Francis K., additional, Cai, Zhaoping, additional, Furcinitti, Paul S., additional, Korn, Alex P., additional, Murali, Ramachandran, additional, and van Oostrum, Jan, additional

Published
1990
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15. Adenovirus Architecture

Author

Burnett, Roger M., Roberts, Michael M., Van Oostrum, Jan, Moras, Dino, editor, Drenth, Jan, editor, Strandberg, Bror, editor, Suck, Dietrich, editor, and Wilson, Keith, editor

Published
1987
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18. Structure of the semiquinone form of flavodoxin from Clostridium MP Extension of 1.8 A resolution and some comparisons with the oxidized state.

Author

Biophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, Mich. 48109, U.S.A., Smith, Ward W., Burnett, Roger M., Darling, George D., Ludwig, Martha L., Biophysics Research Division and Department of Biological Chemistry University of Michigan, Ann Arbor, Mich. 48109, U.S.A., Smith, Ward W., Burnett, Roger M., Darling, George D., and Ludwig, Martha L.

Abstract

As part of a series of comparisons of the structures of the three oxidation states of flavodoxin from Clostridium MP, phases for the semiquinono form were determined to 2.0 A resolution by isomorphous replacement (m> = 0.725). Subsequently, the structure was refined at 1.8 A resolution by a combination of difference Fourier, real space and reciprocal space methods. After refining to an R of 0.194, we explored the conformation of the FMN binding site by real space refinement versus maps with Fourier coefficients of the form (2|Fo|- |Fc|) exp (i[alpha]c). To minimize bias in the fitting, groups of atoms were systematically omitted from the structure factors used in computation of the (2|Fo - |Fc|) maps. One-electron reduction of oxidized flavodoxin is accompanied by several changes at the FMN binding site: the conformation of residues in the reverse bend formed by Met56-Gly57-Asp58-Glu59 differs in the crystal structures of the oxidized and semiquinone species; further, backbone atoms in residues 55 and 89 shift by more than 0.5 A and the indole ring of Trp90 undergoes a significant displacement. The orientation of the peptide unit connecting Gly57 and Asp58 is consistent with the presence of a hydrogen bond between the carbonyl oxygen of Gly57 and the flavin N(5) in flavodoxin semiquinone. No equivalent bond is found in oxidized flavodoxin. In both the oxidized and semiquinone species of clostridial flavodoxin, the isoalloxazine ring is essentially planar : the bending angles about N(5)---N(10) are ~2.5 [deg] for the semiquinone structure and ~0 [deg] in oxidized flavodoxin. The intensity changes resulting from the oxidized agsemiquinone conversion (RI = 0.33) arise in part from changes in molecular packing. Intermolecular contacts, including neighbors of the prosthetic group, are altered in the repacking. Maps or models of the two oxidation states can be brought into approximate coincidence by a rigid body motion. The required transformation, determined for the is

Published
2006

26. Large-Scale Purification and Crystallization of Adenovirus Hexon.

Author

Walker, John M., Wold, William S. M., Tollefson, Ann E., Rux, John J., and Burnett, Roger M.

Abstract

This chapter provides a protocol for the large-scale purification of adenovirus type 2 and 5 virions and the soluble major coat protein hexon. The purified virus particles remain intact and are suitable for vector, vaccine, or structural studies and can also be used as seed stock for further rounds of infection. The hexon may be used to produce crystals suitable for high-resolution X-ray crystallographic studies. Briefly, virus is propagated in HeLa cell suspension cultures. The infected cells are lysed, virions and hexon are separated by centrifugation, and the protein is then further purified by anion exchange chromatography. The entire purification procedure takes approx 1 wk and typically yields 1013 virus particles and 10-20 mg of highly purified hexon. [ABSTRACT FROM AUTHOR]

Published
2007
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40. Large-Scale Purification and Crystallization of Adenovirus Hexon.

Author

Walker, John M., Wold, William S. M., Rux, John J., Pascolini, Donatelia, and Burnett, Roger M.

Abstract

Adenovirus, shortly after its discovery in 1953 (1), was one of the first biological entities to be imaged using the electron microscope (EM) (2). Since then, It has been under continuous scrutiny by structural biologists (reviewed inref. 3). The characteristic shape of the adenovirus virion, with its projecting fibers, made it a fascinating object for early EM studies, which focused on how its > 1O structural proteins are organized to form the virion. The size of the virion, with a diameter of 914å at the fivefold vertices (4) and a mass of over 150 × 1O6 Dalton, presents a formidable challenge for X-ray crystallographic studies. [ABSTRACT FROM AUTHOR]

Published
1998
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45. The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 Å resolution.

Author

Benson, Stacy D., Bamford, Jaana K.H., Bamford, Dennis H., and Burnett, Roger M.

Subjects
VIRAL proteins, PROTEINS, BACTERIOPHAGES, X-ray crystallography, LIPIDS, SYNCHROTRON radiation
Abstract

P3 has been imaged with X-ray crystallography to reveal a trimeric molecule with strikingly similar characteristics to hexon, the major coat protein of adenovirus. The structure of native P3 has now been extended to 1.65 Å resolution (Rwork = 19.0% and Rfree = 20.8%). The new high-resolution model shows that P3 forms crystals through hydrophobic patches solvated by 2-methyl-2,4-pentanediol molecules. It reveals details of how the molecule's high stability may be achieved through ordered solvent in addition to intra- and intersubunit interactions. Of particular importance is a 'puddle' at the top of the molecule containing a four-layer deep hydration shell that cross-links a complex structural feature formed by 'trimerization loops'. These loops also link subunits by extending over a neighbor to reach the third subunit in the trimer. As each subunit has two eight-stranded viral jelly rolls, the trimer has a pseudo-hexagonal shape to allow close packing in its 240 hexavalent capsid positions. Flexible regions in P3 facilitate these interactions within the capsid and with the underlying membrane. A selenomethionine P3 derivative, with which the structure was solved, has been refined to 2.2 Å resolution (Rwork = 20.1% and Rfree = 22.8%). The derivatized molecule is essentially unchanged, although synchrotron radiation has the curious effect of causing it to rotate about its threefold axis. P3 is a second example of a trimeric 'double-barrel' protein that forms a stable building block with optimal shape for constructing a large icosahedral viral capsid. A major difference is that hexon has long variable loops that distinguish different adenovirus species. The short loops in P3 and the severe constraints of its various interactions explain why the PRD1 family has highly conserved coat proteins. [ABSTRACT FROM AUTHOR]

Published
2002
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48. The Crystal Structure of a Fab Fragment to the Melanoma-Associated GD2 Ganglioside

Author

Pichla, Susan L., Murali, Ramachandran, and Burnett, Roger M.

Abstract

The GD2 ganglioside is a cell-surface component that appears on the surface of metastatic melanoma cells and is a marker for the progression of the disease. The ME36.1 monoclonal antibody binds to the GD2 ganglioside and has shown potential as a therapeutic antibody. ME36.1 is a possible alternative therapy to radiation, which is often ineffective in late-stage melanoma. The crystal structure of the Fab fragment of ME36.1 has been determined using molecular replacement and refined to anRfactor of 20.4% at 2.8 Å resolution. The model has good geometry with root-mean-square deviations of 0.008 Å from ideal bond lengths and 1.7° from ideal bond angles. The crystal structure of the ME36.1 Fab shows that its complementarity determining region forms a groove-shaped binding site rather than the pocket-type observed in other sugar binding Fabs. Molecular modeling has placed a four-residue sugar, representative of GD2, in the antigen binding site. The GD2 sugar moiety is stabilized by a network of hydrogen bonds that define the specificity of ME36.1 toward its antigen.

Published
1997
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49. The Structure of the Oxidized Form of Clostridial Flavodoxin at 1.9-A Resolution

Author

Burnett, Roger M., Darling, George D., Kendall, Douglas S., LeQuesne, Mary E., Mayhew, Stephen G., Smith, Ward W., and Ludwig, Martha L.

Abstract

An electron density map of the oxidized form of flavodoxin from Clostridiumstrain MP has been calculated to a resolution of 1.9 A employing isomorphous and anomalous scattering data from two heavy atom derivatives, Smiiiand Aui. In the region from 3.0 to 1.9 A, the largest structure amplitudes (85% of the total | F| s) have been included in the computation. The over-all figure of merit is 0.808. The molecular model resulting from interpretation of this map has a chain length of 138 residues, in accord with the sequence (Tanaka, M., Haniu, M., Yasunobu, K. T., andMayhew, S. G. (1974) J. Biol. Chem.249, 4393–4396). As reported earlier, the molecule possesses a high degree of secondary structure, including a central parallel sheet and four helices. More than 70% of the residues appear to participate in backbone hydrogen bonding. Atomic coordinates, incorporating the sequence data, have been optimized by use of Diamond's model-building program.

Published
1974
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