2gz2
From Proteopedia
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|SITE= <scene name='pdbsite=AC1:A2p+Binding+Site+For+Residue+B+501'>AC1</scene> and <scene name='pdbsite=AC2:A2p+Binding+Site+For+Residue+A+502'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:A2p+Binding+Site+For+Residue+B+501'>AC1</scene> and <scene name='pdbsite=AC2:A2p+Binding+Site+For+Residue+A+502'>AC2</scene> | ||
|LIGAND= <scene name='pdbligand=A2P:ADENOSINE-2'-5'-DIPHOSPHATE'>A2P</scene> | |LIGAND= <scene name='pdbligand=A2P:ADENOSINE-2'-5'-DIPHOSPHATE'>A2P</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] </span> |
|GENE= asd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | |GENE= asd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2gz1|2GZ1]], [[2gyy|2GYY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gz2 OCA], [http://www.ebi.ac.uk/pdbsum/2gz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gz2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Liu, X.]] | [[Category: Liu, X.]] | ||
[[Category: Viola, R E.]] | [[Category: Viola, R E.]] | ||
| - | [[Category: A2P]] | ||
[[Category: aspartate pathway]] | [[Category: aspartate pathway]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:23:11 2008'' |
Revision as of 00:23, 31 March 2008
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| , resolution 2.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Gene: | asd (Streptococcus pneumoniae) | ||||||
| Activity: | Aspartate-semialdehyde dehydrogenase, with EC number 1.2.1.11 | ||||||
| Related: | 2GZ1, 2GYY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with 2',5'-ADP
Overview
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.
About this Structure
2GZ2 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
Examination of key intermediates in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase from a gram-positive infectious bacteria., Faehnle CR, Le Coq J, Liu X, Viola RE, J Biol Chem. 2006 Oct 13;281(41):31031-40. Epub 2006 Aug 8. PMID:16895909
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