2yep
From Proteopedia
(Difference between revisions)
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<StructureSection load='2yep' size='340' side='right' caption='[[2yep]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2yep' size='340' side='right' caption='[[2yep]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [http://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]. <br> | + | <table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YEP FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TH5:O-ACETYL-L-THREONINE'>TH5</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TH5:O-ACETYL-L-THREONINE'>TH5</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzk|2vzk]], [[1vz8|1vz8]], [[2w4n|2w4n]], [[1vz6|1vz6]], [[1vz7|1vz7]], [[2v4i|2v4i]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzk|2vzk]], [[1vz8|1vz8]], [[2w4n|2w4n]], [[1vz6|1vz6]], [[1vz7|1vz7]], [[2v4i|2v4i]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_N-acetyltransferase Glutamate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.35 2.3.1.35] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [http://www.ebi.ac.uk/pdbsum/2yep PDBsum]</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=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [http://www.ebi.ac.uk/pdbsum/2yep PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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[[Category: Glutamate N-acetyltransferase]] | [[Category: Glutamate N-acetyltransferase]] | ||
[[Category: Streptomyces clavuligerus]] | [[Category: Streptomyces clavuligerus]] | ||
| - | [[Category: Chowdhury, R | + | [[Category: Chowdhury, R]] |
| - | [[Category: Clifton, I J | + | [[Category: Clifton, I J]] |
| - | [[Category: Iqbal, A | + | [[Category: Iqbal, A]] |
| - | [[Category: Schofield, C J | + | [[Category: Schofield, C J]] |
[[Category: Acyl enzyme]] | [[Category: Acyl enzyme]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
Revision as of 17:47, 25 December 2014
STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE
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