View source for 7vt1


==Acyltransferase from the 9th Module of Salinomycin Polyketide Synthase==
<StructureSection load='7vt1' size='340' side='right'caption='[[7vt1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vt1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus_subsp._albus Streptomyces albus subsp. albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VT1 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]] 2.5&#8491;</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=7vt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vt1 OCA], [https://pdbe.org/7vt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7vt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vt1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H6D573_STRA4 H6D573_STRA4] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transient protein-protein interactions between cis-acting acyltransferase (AT) and acyl carrier protein (ACP) domains are critical for the catalysis and processivity of modular polyketide synthases (mPKSs), but are challenging for structural characterization due to the intrinsically weak binding affinity. Here, a stable complex of cis-acting AT and ACP domains from the ninth module of the salinomycin mPKS was obtained using a maleimide cross-linker and the structure of the complex was determined at 2.6 A resolution. The crystal structure shows that the AT in combination with the ketosynthase (KS)-to-AT linker forms a C-shaped architecture to embrace the ACP. The large hydrolase subdomain of the AT serves as a major binding platform for the ACP, while the small ferredoxin-like subdomain of the AT and the KS-to-AT linker cooperate with each other to constrain binding of the ACP. The importance of interface residues in cis-acting AT-ACP interactions was confirmed by mutagenesis assays. The interaction mode observed in the cis-acting AT-ACP complex is completely different from those observed in trans-acting AT-ACP complexes, where the ACP primarily contacts the small domain of the AT. The complex structure provides detailed mechanistic insights into AT-ACP recognition in cis-AT mPKSs.

Structural visualization of transient interactions between the cis-acting acyltransferase and acyl carrier protein of the salinomycin modular polyketide synthase.,Feng Y, Zhang F, Huang S, Deng Z, Bai L, Zheng J Acta Crystallogr D Struct Biol. 2022 Jun 1;78(Pt 6):779-791. doi:, 10.1107/S2059798322004612. Epub 2022 May 25. PMID:35647924<ref>PMID:35647924</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vt1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces albus subsp. albus]]
[[Category: Feng Y]]
[[Category: Zhang F]]
[[Category: Zheng J]]