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Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2006 Aug 01; Vol. 62 (Pt 8), pp. 727-30. Date of Electronic Publication: 2006 Jul 29. - Publication Year :
- 2006
-
Abstract
- The crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase (apo-GAPDH) from Synechococcus PCC 7942 is reported. The crystal structure was solved by molecular replacement and refined to an R of 21.7% and R(free) of 27.5% at 2.9 angstroms resolution. The structural features of apo-GAPDH are as follows. The S-loop has an extremely flexible conformation and the sulfate ion is only taken into the classical P(i) site. A structural comparison with holo-GAPDHs indicated that the S-loop fixation is essential in the discrimination of NADP and NAD molecules.
- Subjects :
- Apoenzymes chemistry
Apoenzymes metabolism
Bacterial Proteins chemistry
Crystallography, X-Ray
Glyceraldehyde-3-Phosphate Dehydrogenases metabolism
Models, Molecular
NAD chemistry
NAD metabolism
NADP chemistry
NADP metabolism
Protein Structure, Secondary
Substrate Specificity
Glyceraldehyde-3-Phosphate Dehydrogenases chemistry
Synechococcus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 62
- Issue :
- Pt 8
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 16880542
- Full Text :
- https://doi.org/10.1107/S1744309106027916