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5czc

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The structure of VinK

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 <StructureSection load='5czc' size='340' side='right'caption='[[5czc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5czc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_halstedii"_waksman_and_curtis_1916 "actinomyces halstedii" waksman and curtis 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CZC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5czc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CZC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vinK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1944 "Actinomyces halstedii" Waksman and Curtis 1916])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<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=5czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5czc OCA], [http://pdbe.org/5czc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5czc RCSB], [http://www.ebi.ac.uk/pdbsum/5czc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5czc ProSAT]</span></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=5czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5czc OCA], [https://pdbe.org/5czc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5czc RCSB], [https://www.ebi.ac.uk/pdbsum/5czc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5czc ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q76KY5_STRHA Q76KY5_STRHA]
-Acyltransferases (ATs) are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between AT and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by AT is not understood in detail. Herein, we report the crystal structure of AT VinK, which transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. The isolated VinK structure showed a unique substrate-binding pocket for the dipeptide group linked to ACP. To gain greater insight into the mechanism of ACP recognition, we attempted to crystallize the VinK-ACP complexes. Because transient enzyme-ACP complexes are difficult to crystallize, we developed a covalent cross-linking strategy using a bifunctional maleimide reagent to trap the VinK-ACP complexes, allowing the determination of the crystal structure of the VinK-VinL complex. In the complex structure, Arg-153, Met-206, and Arg-299 of VinK interact with the negatively charged helix II region of VinL. The VinK-VinL complex structure allows, to our knowledge, the first visualization of the interaction between AT and ACP and provides detailed mechanistic insights into ACP recognition by AT.
-Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.,Miyanaga A, Iwasawa S, Shinohara Y, Kudo F, Eguchi T Proc Natl Acad Sci U S A. 2016 Feb 16;113(7):1802-7. doi:, 10.1073/pnas.1520042113. Epub 2016 Feb 1. PMID:26831085<ref>PMID:26831085</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5czc" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Actinomyces halstedii waksman and curtis 1916]]
 [[Category: Large Structures]]
-[[Category: Eguchi, T]]
+[[Category: Streptomyces halstedii]]
-[[Category: Iwasawa, S]]
+[[Category: Eguchi T]]
-[[Category: Kudo, F]]
+[[Category: Iwasawa S]]
-[[Category: Miyanaga, A]]
+[[Category: Kudo F]]
-[[Category: Shinohara, Y]]
+[[Category: Miyanaga A]]
-[[Category: Polyketide biosynthesis]]
+[[Category: Shinohara Y]]
-[[Category: Transferase]]

5czc

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The structure of VinK

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