7f28: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7f28]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_NCGM_237 Acinetobacter baumannii NCGM 237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F28 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f28]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_NCGM_237 Acinetobacter baumannii NCGM 237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F28 FirstGlance]. <br> | ||
</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=7f28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f28 OCA], [https://pdbe.org/7f28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f28 RCSB], [https://www.ebi.ac.uk/pdbsum/7f28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f28 ProSAT]</span></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]] 1.877Å</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=7f28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f28 OCA], [https://pdbe.org/7f28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f28 RCSB], [https://www.ebi.ac.uk/pdbsum/7f28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f28 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 20:08, 29 November 2023
Crystal structure of a bacterial ketosynthaseCrystal structure of a bacterial ketosynthase
Structural highlights
FunctionPublication Abstract from PubMedAryl polyenes (APE) are one of the most widespread secondary metabolites among gram-negative bacteria. In Acinetobacter baumannii, strains belonging to the virulent global clone 2 (GC2) mostly contain APE biosynthesis genes; its relevance in elevated pathogenicity is of great interest. APE biosynthesis gene clusters harbor two ketosynthases (KSs): the heterodimeric KS-chain length factor complex, ApeO-ApeC, and the homodimeric ketoacyl-acyl carrier protein synthase I (FabB)-like KS, ApeR. The role of the two KSs in APE biosynthesis is unclear. We determined the crystal structures of the two KSs from a pathogenic A. baumannii strain. ApeO-ApeC and ApeR have similar cavity volumes; however, ApeR has a narrow cavity near the entrance. In vitro assay based on the absorption characteristics of polyene species indicated the generation of fully elongated polyene with only ApeO-ApeC, probably because of the funnel shaped active site cavity. However, adding ApeR to the reaction increases the throughput of APE biosynthesis. Mutagenesis at Tyr135 in the active site cavity of ApeR reduces the activity significantly, which suggests that the stacking of the aryl group between Tyr135 and Phe202 is important for substrate recognition. Therefore, the two KSs function complementarily in the generation of APE to enhance its production. Structural basis of the complementary activity of two ketosynthases in aryl polyene biosynthesis.,Lee WC, Choi S, Jang A, Yeon J, Hwang E, Kim Y Sci Rep. 2021 Aug 11;11(1):16340. doi: 10.1038/s41598-021-95890-y. PMID:34381152[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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