View source for 2yep


==STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE==
<StructureSection load='2yep' size='340' side='right'caption='[[2yep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w4n 2w4n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEP 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=TH5:O-ACETYL-L-THREONINE'>TH5</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=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [https://pdbe.org/2yep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [https://www.ebi.ac.uk/pdbsum/2yep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yep ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GNAT2_STRCL GNAT2_STRCL] Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors.<ref>PMID:11985581</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.

Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.,Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301<ref>PMID:21796301</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yep" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces clavuligerus]]
[[Category: Chowdhury R]]
[[Category: Clifton IJ]]
[[Category: Iqbal A]]
[[Category: Schofield CJ]]