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4i49
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of ngNAGS bound with bisubstrate analog CoA-NAG== | |
| + | <StructureSection load='4i49' size='340' side='right'caption='[[4i49]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4i49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_SK-93-1035 Neisseria gonorrhoeae SK-93-1035]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I49 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1C4:(2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]-3,5,9-TRIHYDROXY-8,8-DIMETHYL-3,5-DIOXIDO-10,14,20-TRIOXO-2,4,6-TRIOXA-18-THIA-11,15-DIAZA-3LAMBDA~5~,5LAMBDA~5~-DIPHOSPHAICOSAN-20-YL}AMINO)PENTANEDIOIC+ACID+(NON-PREFERRED+NAME)'>1C4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i49 OCA], [https://pdbe.org/4i49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i49 RCSB], [https://www.ebi.ac.uk/pdbsum/4i49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i49 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N-Acetyl-l-glutamate synthase catalyzes the conversion of AcCoA and glutamate to CoA and N-acetyl-l-glutamate (NAG), the first step of the arginine biosynthetic pathway in lower organisms. In mammals, NAG is an obligate cofactor of carbamoyl phosphate synthetase I in the urea cycle. We have previously reported the structures of NAGS from Neisseria gonorrhoeae (ngNAGS) with various substrates bound. Here we reported the preparation of the bisubstrate analog, CoA-S-acetyl-l-glutamate, the crystal structure of ngNAGS with CoA-NAG bound, and kinetic studies of several active site mutants. The results are consistent with a one-step nucleophilic addition-elimination mechanism with Glu353 as the catalytic base and Ser392 as the catalytic acid. The structure of the ngNAGS-bisubstrate complex together with the previous ngNAGS structures delineates the catalytic reaction path for ngNAGS. | ||
| - | + | Structure of the complex of Neisseria gonorrhoeae N-acetyl-l-glutamate synthase with a bound bisubstrate analog.,Zhao G, Allewell NM, Tuchman M, Shi D Biochem Biophys Res Commun. 2012 Dec 20. pii: S0006-291X(12)02412-6. doi:, 10.1016/j.bbrc.2012.12.064. PMID:23261468<ref>PMID:23261468</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4i49" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neisseria gonorrhoeae SK-93-1035]] | ||
| + | [[Category: Allewell NM]] | ||
| + | [[Category: Shi D]] | ||
| + | [[Category: Tuchman M]] | ||
| + | [[Category: Zhao G]] | ||
Current revision
Structure of ngNAGS bound with bisubstrate analog CoA-NAG
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