7f27: Difference between revisions
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==Crystal structure of polyketide ketosynthase== | ==Crystal structure of polyketide ketosynthase== | ||
<StructureSection load='7f27' size='340' side='right'caption='[[7f27]]' scene=''> | <StructureSection load='7f27' size='340' side='right'caption='[[7f27]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F27 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f27]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ACICU Acinetobacter baumannii ACICU]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F27 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=7f27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f27 OCA], [https://pdbe.org/7f27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f27 RCSB], [https://www.ebi.ac.uk/pdbsum/7f27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f27 ProSAT]</span></td></tr> | </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=7f27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f27 OCA], [https://pdbe.org/7f27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f27 RCSB], [https://www.ebi.ac.uk/pdbsum/7f27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f27 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7U3XWE2_ACIBC A0A7U3XWE2_ACIBC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aryl 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<ref>PMID:34381152</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7f27" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acinetobacter baumannii ACICU]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim Y]] | [[Category: Kim Y]] | ||
[[Category: Lee WC]] | [[Category: Lee WC]] |
Revision as of 12:13, 28 December 2022
Crystal structure of polyketide ketosynthaseCrystal structure of polyketide 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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