4i49
From Proteopedia
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| - | [[ | + | ==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I49 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d2m|3d2m]], [[3b8g|3b8g]], [[2r2v|2r2v]], [[3d2p|3d2p]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argA, NGLG_00316 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=528360 Neisseria gonorrhoeae SK-93-1035])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amino-acid_N-acetyltransferase Amino-acid N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.1 2.3.1.1] </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=4i49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i49 RCSB], [http://www.ebi.ac.uk/pdbsum/4i49 PDBsum]</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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Amino-acid N-acetyltransferase]] | [[Category: Amino-acid N-acetyltransferase]] | ||
[[Category: Neisseria gonorrhoeae sk-93-1035]] | [[Category: Neisseria gonorrhoeae sk-93-1035]] | ||
| - | [[Category: Allewell, N M | + | [[Category: Allewell, N M]] |
| - | [[Category: Shi, D | + | [[Category: Shi, D]] |
| - | [[Category: Tuchman, M | + | [[Category: Tuchman, M]] |
| - | [[Category: Zhao, G | + | [[Category: Zhao, G]] |
[[Category: Protein-bisubstrate analog complex]] | [[Category: Protein-bisubstrate analog complex]] | ||
[[Category: Synthase]] | [[Category: Synthase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 17:00, 10 December 2014
Structure of ngNAGS bound with bisubstrate analog CoA-NAG
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