2GYY: Structure Of Aspartate Semialdehyde Dehydrogenase (Asadh) From Streptococcus Pneumoniae

Citation:
Abstract
Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes a critical branch point transformation in amino acid bio-synthesis. The products of the aspartate pathway are essential in microorganisms, and this entire pathway is absent in mammals, making this enzyme an attractive target for antibiotic development. The first structure of an ASADH from a Gram-positive bacterium, Streptococcus pneumoniae, has now been determined. The overall structure of the apoenzyme has a similar fold to those of the Gram-negative and archaeal ASADHs but contains some interesting structural variations that can be exploited for inhibitor design. Binding of the coenzyme NADP, as well as a truncated nucleotide analogue, into an alternative conformation from that observed in Gram-negative ASADHs causes an enzyme domain closure that precedes catalysis. The covalent acyl-enzyme intermediate was trapped by soaking the substrate into crystals of the coenzyme complex, and the structure of this elusive intermediate provides detailed insights into the catalytic mechanism.
PDB ID: 2GYYDownload
MMDB ID: 40955
PDB Deposition Date: 2006/5/10
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2GYY: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2GYY
Label Count Molecule
Proteins (2 molecules)
2
Aspartate Beta-semialdehyde Dehydrogenase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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