7f2r: Difference between revisions
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==== | ==Crystal structure of VinK-VinL covalent complex formed with a pantetheineamide cross-linking probe== | ||
<StructureSection load='7f2r' size='340' side='right'caption='[[7f2r]]' scene=''> | <StructureSection load='7f2r' size='340' side='right'caption='[[7f2r]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f2r]] is a 4 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=7F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F2R FirstGlance]. <br> | ||
</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=7f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f2r OCA], [https://pdbe.org/7f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f2r RCSB], [https://www.ebi.ac.uk/pdbsum/7f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f2r ProSAT]</span></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]] 1.95Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9EF:N-[2-(acetylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide'>9EF</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=7f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f2r OCA], [https://pdbe.org/7f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f2r RCSB], [https://www.ebi.ac.uk/pdbsum/7f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f2r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q76KY5_STRHA Q76KY5_STRHA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Acyltransferases are responsible for the selection and loading of acyl units onto carrier proteins in polyketide and fatty-acid biosynthesis. Despite the importance of protein-protein interactions between the acyltransferase and the carrier protein, structural information on acyltransferase-carrier protein interactions is limited because of the transient interactions between them. In the biosynthesis of the polyketide vicenistatin, the acyltransferase VinK recognizes the carrier protein VinL for the transfer of a dipeptidyl unit. The crystal structure of a VinK-VinL covalent complex formed with a 1,2-bismaleimidoethane cross-linking reagent has been determined previously. Here, the crystal structure of a VinK-VinL covalent complex formed with a pantetheine cross-linking probe is reported at 1.95 A resolution. In the structure of the VinK-VinL-probe complex, the pantetheine probe that is attached to VinL is covalently connected to the side chain of the mutated Cys106 of VinK. The interaction interface between VinK and VinL is essentially the same in the two VinK-VinL complex structures, although the position of the pantetheine linker slightly differs. This structural observation suggests that interface interactions are not affected by the cross-linking strategy used. | |||
Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.,Miyanaga A, Ouchi R, Kudo F, Eguchi T Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):294-302. doi:, 10.1107/S2053230X21008761. Epub 2021 Aug 26. PMID:34473106<ref>PMID:34473106</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7f2r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces halstedii]] | ||
[[Category: Eguchi T]] | |||
[[Category: Kudo F]] | |||
[[Category: Miyanaga A]] | |||
[[Category: Ouchi R]] | |||
Latest revision as of 20:08, 29 November 2023
Crystal structure of VinK-VinL covalent complex formed with a pantetheineamide cross-linking probeCrystal structure of VinK-VinL covalent complex formed with a pantetheineamide cross-linking probe
Structural highlights
FunctionPublication Abstract from PubMedAcyltransferases are responsible for the selection and loading of acyl units onto carrier proteins in polyketide and fatty-acid biosynthesis. Despite the importance of protein-protein interactions between the acyltransferase and the carrier protein, structural information on acyltransferase-carrier protein interactions is limited because of the transient interactions between them. In the biosynthesis of the polyketide vicenistatin, the acyltransferase VinK recognizes the carrier protein VinL for the transfer of a dipeptidyl unit. The crystal structure of a VinK-VinL covalent complex formed with a 1,2-bismaleimidoethane cross-linking reagent has been determined previously. Here, the crystal structure of a VinK-VinL covalent complex formed with a pantetheine cross-linking probe is reported at 1.95 A resolution. In the structure of the VinK-VinL-probe complex, the pantetheine probe that is attached to VinL is covalently connected to the side chain of the mutated Cys106 of VinK. The interaction interface between VinK and VinL is essentially the same in the two VinK-VinL complex structures, although the position of the pantetheine linker slightly differs. This structural observation suggests that interface interactions are not affected by the cross-linking strategy used. Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.,Miyanaga A, Ouchi R, Kudo F, Eguchi T Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):294-302. doi:, 10.1107/S2053230X21008761. Epub 2021 Aug 26. PMID:34473106[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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