View source for 7vwk


==The product template domain of AviM==
<StructureSection load='7vwk' size='340' side='right'caption='[[7vwk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vwk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridochromogenes_Tue57 Streptomyces viridochromogenes Tue57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VWK 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&#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=7vwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vwk OCA], [https://pdbe.org/7vwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vwk RCSB], [https://www.ebi.ac.uk/pdbsum/7vwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vwk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/L8PIV2_STRVR L8PIV2_STRVR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The product template (PT) domains act as an aldol cyclase to control the regiospecific aldol cyclization of the extremely reactive poly-beta-ketone intermediate assembled by an iterative type I polyketide synthases (PKSs). Up to now, only the structure of fungal PksA PT that mediates the first-ring cyclization via C4-C9 aldol cyclization is available. We describe here the structural and computational characterization of a bacteria PT domain that controls C2-C7 cyclization in orsellinic acid (OSA) synthesis. Mutating the catalytic H949 of the PT abolishes production of OSA and results in a tetraacetic acid lactone (TTL) generated by spontaneous O-C cyclization of the acyl carrier protein (ACP)-bound tetraketide intermediate. Crystal structure of the bacterial PT domain closely resembles dehydrase (DH) domains of modular type I PKSs in the overall fold, dimerization interface and His-Asp catalytic dyad organization, but is significantly different from PTs of fungal iterative type I PKSs. QM/MM calculation suggests that the catalytic H949 abstracts a proton from C2 and transfers it to C7 carbonyl to mediate the cyclization reaction. According to structural similarity to DHs and functional similarity to fungal PTs, we propose that the bacterial PT represents an evolutionary intermediate between the two tailoring domains of type I PKSs.

The Streptomyces viridochromogenes product template domain represents an evolutionary intermediate between dehydratase and aldol cyclase of type I polyketide synthases.,Feng Y, Yang X, Ji H, Deng Z, Lin S, Zheng J Commun Biol. 2022 May 26;5(1):508. doi: 10.1038/s42003-022-03477-8. PMID:35618872<ref>PMID:35618872</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vwk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces viridochromogenes Tue57]]
[[Category: Feng Y]]
[[Category: Yang X]]
[[Category: Zheng J]]