This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4ylt
From Proteopedia
(Difference between revisions)
m (Protected "4ylt" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | ''' | + | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YLT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </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=4ylt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ylt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ylt RCSB], [http://www.ebi.ac.uk/pdbsum/4ylt PDBsum]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | [[Category: Forwood, J | + | [[http://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. |
| - | [[Category: Nanson, J | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Forwood, J K]] | ||
| + | [[Category: Nanson, J D]] | ||
| + | [[Category: Condensing enzyme]] | ||
| + | [[Category: Fabh]] | ||
| + | [[Category: Fatty acid biosynthesis]] | ||
| + | [[Category: Thiolase fold]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 11:19, 8 April 2015
Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis
| |||||||||||
