8i4z: Difference between revisions
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The | ==CalA3 with hydrolysis product== | ||
<StructureSection load='8i4z' size='340' side='right'caption='[[8i4z]], [[Resolution|resolution]] 3.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8i4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_chartreusis_NRRL_3882 Streptomyces chartreusis NRRL 3882]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I4Z FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.97Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ONF:11-oxidanylidene-11-(1~{H}-pyrrol-2-yl)undecanoic+acid'>ONF</scene></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=8i4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i4z OCA], [https://pdbe.org/8i4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i4z RCSB], [https://www.ebi.ac.uk/pdbsum/8i4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i4z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2N9BJK0_STRCX A0A2N9BJK0_STRCX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Assembly-line polyketide synthases (PKSs) are molecular factories that produce diverse metabolites with wide-ranging biological activities. PKSs usually work by constructing and modifying the polyketide backbone successively. Here, we present the cryo-EM structure of CalA3, a chain release PKS module without an ACP domain, and its structures with amidation or hydrolysis products. The domain organization reveals a unique "infinity"-shaped dimeric architecture with five connected domains. The catalytic region tightly contacts the structural region, resulting in two stabilized chambers with nearly perfect symmetry while the N-terminal docking domain is flexible. The structures of the ketosynthase (KS) domain illustrate how the conserved key residues that canonically catalyze C-C bond formation can be tweaked to mediate C-N bond formation, revealing the engineering adaptability of assembly-line polyketide synthases for the production of novel pharmaceutical agents. | |||
C-N bond formation by a polyketide synthase.,Wang J, Wang X, Li X, Kong L, Du Z, Li D, Gou L, Wu H, Cao W, Wang X, Lin S, Shi T, Deng Z, Wang Z, Liang J Nat Commun. 2023 Mar 10;14(1):1319. doi: 10.1038/s41467-023-36989-w. PMID:36899013<ref>PMID:36899013</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8i4z" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces chartreusis NRRL 3882]] | |||
[[Category: Wang J]] | |||
[[Category: Wang Z]] | |||