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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/As_4.1611 As 4.1611]. 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> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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 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='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 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> |
| - | <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 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://pdbe.org/2yep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [http://www.ebi.ac.uk/pdbsum/2yep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yep ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 4 1611]] | |
| - | [[Category: Glutamate N-acetyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chowdhury, R]] | + | [[Category: Streptomyces clavuligerus]] |
| - | [[Category: Clifton, I J]] | + | [[Category: Chowdhury R]] |
| - | [[Category: Iqbal, A]] | + | [[Category: Clifton IJ]] |
| - | [[Category: Schofield, C J]] | + | [[Category: Iqbal A]] |
| - | [[Category: Acyl enzyme]] | + | [[Category: Schofield CJ]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ntn hydrolase]]
| + | |
| - | [[Category: Ornithine acetyl transferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kershaw NJ, McNaughton HJ, Hewitson KS, Hernandez H, Griffin J, Hughes C, Greaves P, Barton B, Robinson CV, Schofield CJ. ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity. Eur J Biochem. 2002 Apr;269(8):2052-9. PMID:11985581
- ↑ Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ. Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates. Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301 doi:10.1039/c1ob05554b
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