View source for 6l3n


==Crystal Structure of the acyltransferase domain from the third module of the ansamitocin polyketide synthase==
<StructureSection load='6l3n' size='340' side='right'caption='[[6l3n]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l3n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinosynnema_pretiosum_subsp._auranticum Actinosynnema pretiosum subsp. auranticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L3N 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]] 1.83&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DXX:METHYLMALONIC+ACID'>DXX</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l3n OCA], [https://pdbe.org/6l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l3n RCSB], [https://www.ebi.ac.uk/pdbsum/6l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l3n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1U9Y7T8_9PSEU A0A1U9Y7T8_9PSEU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A few acyltransferase (AT) domains of modular polyketide synthases (PKSs) recruit acyl carrier protein (ACP)-linked extender units with unusual C2 substituents to confer functionalities that are not available in coenzyme A (CoA)-linked ones. Here, an AT specific for methoxymalonyl (MOM)-ACP in the third module of the ansamitocin PKS was structurally and biochemically characterized. The AT uses a conserved tryptophan at the entrance of the substrate binding tunnel to discriminate between different carriers. A W275R mutation switches its carrier specificity from the ACP protein to the CoA molecule. The acyl-AT complex structures clearly show that the MOM-ACP accepted by the AT has the 2S instead of the opposite 2R stereochemistry that is predicted according to the biosynthetic derivation from a D-glycolytic intermediate. Together, these results reveal the structural basis of ATs recognizing ACP-linked extender units in polyketide biosynthesis.

Structural and Biochemical insights to the Recruitment of Acyl Carrier Protein-linked Extender Units in Ansamitocin Biosynthesis.,Zhang F, Ji H, Ali I, Deng Z, Bai L, Zheng J Chembiochem. 2019 Nov 27. doi: 10.1002/cbic.201900628. PMID:31777147<ref>PMID:31777147</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6l3n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinosynnema pretiosum subsp. auranticum]]
[[Category: Large Structures]]
[[Category: Zhang F]]
[[Category: Zheng J]]