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| | <StructureSection load='2v4i' size='340' side='right'caption='[[2v4i]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2v4i' size='340' side='right'caption='[[2v4i]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v4i]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V4I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2V4I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v4i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V4I FirstGlance]. <br> |
| | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene></td></tr> | | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzk|2vzk]], [[1vz8|1vz8]], [[1vz6|1vz6]], [[1vz7|1vz7]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vzk|2vzk]], [[1vz8|1vz8]], [[1vz6|1vz6]], [[1vz7|1vz7]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_N-acetyltransferase Glutamate N-acetyltransferase], with EC number [https://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://proteopedia.org/fgij/fg.htm?mol=2v4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v4i OCA], [http://pdbe.org/2v4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v4i RCSB], [http://www.ebi.ac.uk/pdbsum/2v4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v4i ProSAT]</span></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=2v4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v4i OCA], [https://pdbe.org/2v4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v4i RCSB], [https://www.ebi.ac.uk/pdbsum/2v4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v4i 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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The orf6 gene from the clavulanic acid biosynthesis gene cluster encodes an OAT (ornithine acetyltransferase). Similar to other OATs the enzyme has been shown to catalyse the reversible transfer of an acetyl group from N-acetylornithine to glutamate. OATs are Ntn (N-terminal nucleophile) enzymes, but are distinct from the better-characterized Ntn hydrolase enzymes as they catalyse acetyl transfer rather than a hydrolysis reaction. In the present study, we describe the X-ray crystal structure of the OAT, corresponding to the orf6 gene product, to 2.8 A (1 A=0.1 nm) resolution. The larger domain of the structure consists of an alphabetabetaalpha sandwich as in the structures of Ntn hydrolase enzymes. However, differences in the connectivity reveal that OATs belong to a structural family different from that of other structurally characterized Ntn enzymes, with one exception: unexpectedly, the alphabetabetaalpha sandwich of ORF6 (where ORF stands for open reading frame) displays the same fold as an DmpA (L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi), and so the OATs and DmpA form a new structural subfamily of Ntn enzymes. The structure reveals an alpha2beta2-heterotetrameric oligomerization state in which the intermolecular interface partly defines the active site. Models of the enzyme-substrate complexes suggest a probable oxyanion stabilization mechanism as well as providing insight into how the enzyme binds its two differently charged substrates.
X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster.,Elkins JM, Kershaw NJ, Schofield CJ Biochem J. 2005 Jan 15;385(Pt 2):565-73. PMID:15352873[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
- ↑ Elkins JM, Kershaw NJ, Schofield CJ. X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster. Biochem J. 2005 Jan 15;385(Pt 2):565-73. PMID:15352873 doi:http://dx.doi.org/10.1042/BJ20040814
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