4ylt
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4ylt is ON HOLD Authors: Nanson, J.D., Forwood, J.K. Description: Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis [...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis== | |
| + | <StructureSection load='4ylt' size='340' side='right'caption='[[4ylt]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ylt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YLT 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]] 2.2Å</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=4ylt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylt OCA], [https://pdbe.org/4ylt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ylt RCSB], [https://www.ebi.ac.uk/pdbsum/4ylt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ylt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABH_YERPE FABH_YERPE] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. | ||
| - | + | ==See Also== | |
| - | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Forwood | + | [[Category: Large Structures]] |
| - | [[Category: Nanson | + | [[Category: Yersinia pestis]] |
| + | [[Category: Forwood JK]] | ||
| + | [[Category: Nanson JD]] | ||
Current revision
Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis
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