3jz4

<StructureSection load='3jz4' size='340' side='right' caption='[[3jz4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[3jz4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JZ4 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2661, gabD, JW2636, NA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate-semialdehyde_dehydrogenase_(NAD(P)(+)) Succinate-semialdehyde dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.16 1.2.1.16] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jz4 OCA], [http://pdbe.org/3jz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jz4 RCSB], [http://www.ebi.ac.uk/pdbsum/3jz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jz4 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GABD_ECOLI GABD_ECOLI]] Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. It appears to be important for nitrogen metabolism under N limitation conditions.<ref>PMID:20174634</ref> <ref>PMID:7011797</ref>

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== Publication Abstract from PubMed ==

BACKGROUND: In mammals succinic semialdehyde dehydrogenase (SSADH) plays an essential role in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) to succinic acid (SA). Deficiency of SSADH in humans results in elevated levels of GABA and gamma-Hydroxybutyric acid (GHB), which leads to psychomotor retardation, muscular hypotonia, non-progressive ataxia and seizures. In Escherichia coli, two genetically distinct forms of SSADHs had been described that are essential for preventing accumulation of toxic levels of succinic semialdehyde (SSA) in cells. METHODOLOGY/PRINCIPAL FINDINGS: Here we structurally characterise SSADH encoded by the E coli gabD gene by X-ray crystallographic studies and compare these data with the structure of human SSADH. In the E. coli SSADH structure, electron density for the complete NADP+ cofactor in the binding sites is clearly evident; these data in particular revealing how the nicotinamide ring of the cofactor is positioned in each active site. CONCLUSIONS/SIGNIFICANCE: Our structural data suggest that a deletion of three amino acids in E. coli SSADH permits this enzyme to use NADP+, whereas in contrast the human enzyme utilises NAD+. Furthermore, the structure of E. coli SSADH gives additional insight into human mutations that result in disease.

The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.,Langendorf CG, Key TL, Fenalti G, Kan WT, Buckle AM, Caradoc-Davies T, Tuck KL, Law RH, Whisstock JC PLoS One. 2010 Feb 18;5(2):e9280. PMID:20174634<ref>PMID:20174634</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3jz4" style="background-color:#fffaf0;"></div>

*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]]

[[Category: Bacillus coli migula 1895]]

[[Category: Buckle, A M]]

[[Category: Caradoc-Davies, T]]

[[Category: Fenalti, G]]

[[Category: Kan, W T]]

[[Category: Key, T L.G]]

[[Category: Langendorf, C G]]

[[Category: Law, R H.P]]

[[Category: Tuck, K L]]

[[Category: Whisstock, J C]]

[[Category: Tetramer]]