6vap: Difference between revisions
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<StructureSection load='6vap' size='340' side='right'caption='[[6vap]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='6vap' size='340' side='right'caption='[[6vap]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6vap]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6vap]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._WAC02707 Streptomyces sp. WAC02707]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VAP FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vap OCA], [https://pdbe.org/6vap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vap RCSB], [https://www.ebi.ac.uk/pdbsum/6vap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vap ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A454WD44_9ACTN A0A454WD44_9ACTN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6vap" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6vap" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thioesterase 3D structures|Thioesterase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Streptomyces sp. | [[Category: Streptomyces sp. WAC02707]] | ||
[[Category: Adams | [[Category: Adams PD]] | ||
[[Category: Baluyot | [[Category: Baluyot M-J]] | ||
[[Category: Curran | [[Category: Curran SC]] | ||
[[Category: Keasling | [[Category: Keasling J]] | ||
[[Category: Lake | [[Category: Lake J]] | ||
[[Category: Pereira | [[Category: Pereira JH]] | ||
[[Category: Putz | [[Category: Putz H]] | ||
[[Category: Rosenburg | [[Category: Rosenburg D]] | ||
Latest revision as of 11:07, 11 October 2023
Structure of the type II thioesterase BorB from the borrelidin biosynthetic clusterStructure of the type II thioesterase BorB from the borrelidin biosynthetic cluster
Structural highlights
FunctionPublication Abstract from PubMedalpha/beta hydrolases make up a large and diverse protein superfamily. In natural product biosynthesis, cis-acting thioesterase alpha/beta hydrolases can terminate biosynthetic assembly lines and release products by hydrolyzing or cyclizing the biosynthetic intermediate. Thioesterases can also act in trans, removing aberrant intermediates and restarting stalled biosynthesis. Knockout of this "editing" function leads to reduced product titers. The borrelidin biosynthetic gene cluster from Streptomyces parvulus Tu4055 contains a hitherto uncharacterized stand-alone thioesterase, borB. In this work, we demonstrate that purified BorB cleaves acyl substrates with a preference for propionate, which supports the hypothesis that it is also an editing thioesterase. The crystal structure of BorB shows a wedgelike hydrophobic substrate binding crevice that limits substrate length. To investigate the structure-function relationship, we made chimeric BorB variants using loop regions from characterized homologues with different specificities. BorB chimeras slightly reduced activity, arguing that the modified region is a not major determinant of substrate preference. The structure-function relationships described here contribute to the process of elimination for understanding thioesterase specificity and, ultimately, engineering and applying trans-acting thioesterases in biosynthetic assembly lines. Structure and Function of BorB, the Type II Thioesterase from the Borrelidin Biosynthetic Gene Cluster.,Curran SC, Pereira JH, Baluyot MJ, Lake J, Puetz H, Rosenburg DJ, Adams P, Keasling JD Biochemistry. 2020 Apr 28;59(16):1630-1639. doi: 10.1021/acs.biochem.0c00126., Epub 2020 Apr 13. PMID:32250597[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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