6l3m

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'''Unreleased structure'''
 
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The entry 6l3m is ON HOLD
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==Crystal Structure of the acyltransferase domain from the third module of the ansamitocin polyketide synthase==
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<StructureSection load='6l3m' size='340' side='right'caption='[[6l3m]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6l3m]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L3M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L3M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E5U:2-methoxypropanedioic+acid'>E5U</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6l3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l3m OCA], [http://pdbe.org/6l3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l3m RCSB], [http://www.ebi.ac.uk/pdbsum/6l3m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l3m ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Zhang, F., Zheng, J.
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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>
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Description: Crystal Structure of the acyltransferase domain from the third module of the ansamitocin polyketide synthase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zheng, J]]
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<div class="pdbe-citations 6l3m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Zhang, F]]
[[Category: Zhang, F]]
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[[Category: Zheng, J]]
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[[Category: Acp-linked extender unit]]
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[[Category: Acyltransferase]]
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[[Category: Biosynthesis]]
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[[Category: Carrier specificity]]
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[[Category: Polyketide]]
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[[Category: Transferase]]

Revision as of 07:42, 18 December 2019

Crystal Structure of the acyltransferase domain from the third module of the ansamitocin polyketide synthase

PDB ID 6l3m

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