View source for 4kzt


==Structure mmNAGS bound with L-arginine==
<StructureSection load='4kzt' size='340' side='right'caption='[[4kzt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kzt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Maricaulis_maris_MCS10 Maricaulis maris MCS10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KZT 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4kzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kzt OCA], [https://pdbe.org/4kzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kzt RCSB], [https://www.ebi.ac.uk/pdbsum/4kzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kzt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0ASS9_MARMM Q0ASS9_MARMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Maricaulis maris N-acetylglutamate synthase/kinase (mmNAGS/K) catalyzes the first two steps in L-arginine biosynthesis and has a high degree of sequence and structural homology to human N-acetylglutamate synthase, a regulator of the urea cycle. The synthase activity of both mmNAGS/K and human NAGS are regulated by L-arginine, although L-arginine is an allosteric inhibitor of mmNAGS/K, but an activator of human NAGS. To investigate the mechanism of allosteric inhibition of mmNAGS/K by L-arginine, we have determined the structure of the mmNAGS/K complexed with L-arginine at 2.8 A resolution. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations. In this conformation, the AcCoA binding site in the N-acetyltransferase (NAT) domain is blocked by a loop from the amino acid kinase (AAK) domain, as a result of a domain rotation that occurs when L-arginine binds. This structural change provides an explanation for the allosteric inhibition of mmNAGS/K and related enzymes by L-arginine. The allosterically regulated mechanism for mmNAGS/K differs significantly from that for Neisseria gonorrhoeae NAGS (ngNAGS). To define the active site, several residues near the putative active site were mutated and their activities determined. These experiments identify roles for Lys356, Arg386, Asn391 and Tyr397 in the catalytic mechanism.

Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound.,Zhao G, Haskins N, Jin Z, M Allewell N, Tuchman M, Shi D Biochem Biophys Res Commun. 2013 Aug 9;437(4):585-90. doi:, 10.1016/j.bbrc.2013.07.003. Epub 2013 Jul 10. PMID:23850694<ref>PMID:23850694</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kzt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Maricaulis maris MCS10]]
[[Category: Allewell NM]]
[[Category: Jin Z]]
[[Category: Shi D]]
[[Category: Tuchman M]]
[[Category: Zhao G]]