4qlo

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qlo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QLO FirstGlance]. <br>
<table><tr><td colspan='2'>[[4qlo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QLO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span></td></tr>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_O-acetyltransferase Homoserine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.31 2.3.1.31] </span></td></tr>
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<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=4qlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qlo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qlo RCSB], [http://www.ebi.ac.uk/pdbsum/4qlo PDBsum]</span></td></tr>
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<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=4qlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qlo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qlo RCSB], [http://www.ebi.ac.uk/pdbsum/4qlo PDBsum]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Homoserine O-acetyltransferase (HTA) catalyzes the formation of L-O-acetyl-homoserine from L-homoserine through the transfer of an acetyl group from acetyl-CoA. This is the first committed step required for the biosynthesis of methionine in many fungi, Gram-positive bacteria and some Gram-negative bacteria. The structure of HTA from Staphylococcus aureus (SaHTA) has been determined to a resolution of 2.45 A. The structure belongs to the alpha/beta-hydrolase superfamily, consisting of two distinct domains: a core alpha/beta-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel. Structure analysis revealed some important differences for SaHTA compared with the few known structures of HTA.
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Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.,Thangavelu B, Pavlovsky AG, Viola R Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1340-5. doi:, 10.1107/S2053230X14018664. Epub 2014 Sep 25. PMID:25286936<ref>PMID:25286936</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homoserine O-acetyltransferase]]
[[Category: Homoserine O-acetyltransferase]]
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[[Category: Pavlovsky, A G.]]
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[[Category: Pavlovsky, A G]]
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[[Category: Thangavelu, B.]]
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[[Category: Thangavelu, B]]
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[[Category: Viola, R E.]]
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[[Category: Viola, R E]]
[[Category: Acetylco-a binding]]
[[Category: Acetylco-a binding]]
[[Category: Acetyltransferase]]
[[Category: Acetyltransferase]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 08:44, 17 December 2014

Crystal Structure of homoserine o-acetyltransferase from Staphylococcus aureus

4qlo, resolution 2.45Å

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