2gsa
CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM)
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OverviewOverview
The three-dimensional structure of glutamate-1-semialdehyde aminomutase, (EC 5.4.3.8), an alpha2-dimeric enzyme from Synechococcus, has been, determined by x-ray crystallography using heavy atom derivative phasing., The structure, refined at 2.4-A resolution to an R-factor of 18.7% and, good stereochemistry, explains many of the enzyme's unusual specificity, and functional properties. The overall fold is that of aspartate, aminotransferase and related B6 enzymes, but it also has specific, features. The structure of the complex with gabaculine, a substrate, analogue, shows unexpectedly that the substrate binding site involves, residues from the N-terminal domain of the molecule, notably Arg-32., Glu-406 is suitably positioned to repel alpha-carboxylic acids, thereby, suggesting a basis for ... [(full description)]
About this StructureAbout this Structure
2GSA is a [Single protein] structure of sequence from [Synechococcus sp.] with PMP and PLP as [ligands]. Active as [[1]], with EC number [5.4.3.8]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity., Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN, Proc Natl Acad Sci U S A. 1997 May 13;94(10):4866-71. PMID:9144156
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