6kjh: Difference between revisions
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<StructureSection load='6kjh' size='340' side='right'caption='[[6kjh]], [[Resolution|resolution]] 1.68Å' scene=''> | <StructureSection load='6kjh' size='340' side='right'caption='[[6kjh]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6kjh]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6kjh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Jeotgalibacillus_marinus Jeotgalibacillus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KJH 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]] 1.68Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6kjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kjh OCA], [https://pdbe.org/6kjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kjh RCSB], [https://www.ebi.ac.uk/pdbsum/6kjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kjh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0U1X4V6_9BACL A0A0U1X4V6_9BACL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Jeotgalibacillus marinus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feng | [[Category: Feng Y]] | ||
[[Category: Li | [[Category: Li W]] | ||
[[Category: Sheng | [[Category: Sheng D]] | ||
[[Category: Xiao | [[Category: Xiao F]] | ||
Latest revision as of 13:34, 22 November 2023
Functional and structural insights into the unusual oxyanion hole-like geometry in macrolactin acyltransferase selective for dicarboxylic acyl donorsFunctional and structural insights into the unusual oxyanion hole-like geometry in macrolactin acyltransferase selective for dicarboxylic acyl donors
Structural highlights
FunctionPublication Abstract from PubMedMacrolactins (MLNs) are a class of important antimacular degeneration and antitumor agents. Malonylated/succinylated MLNs are even more important due to their efficacy in overcoming multi-drug-resistant bacteria. However, which enzyme catalyzes this reaction remains enigmatic. Herein, we deciphered a beta-lactamase homologue BmmI to be responsible for this step. BmmI could specifically attach C3-C5 alkyl acid thioesters onto 7-OH of MLN A and also exhibits substrate promiscuity toward acyl acceptors with different scaffolds. The crystal structure of BmmI covalently linked to the succinyl group and systematic mutagenesis highlighted the role of oxyanion holelike geometry in the recognition of carboxyl-terminated acyl donors. The engineering of this geometry expanded its substrate scope, with the R166A/G/Q variants recognizing up to C12 alkyl acid thioester. The structure of BmmI with acyl acceptor MLN A revealed the importance of Arg292 in the recognition of macrolide substrates. Moreover, the mechanism of the BmmI-catalyzed acyltransfer reaction was established, unmasking the deft role of Lys76 in governing acyl donors as well as catalysis. Our studies uncover the delicate mechanism underlying the substrate selectivity of acyltransferases, which would guide rational enzyme engineering for drug development. Structural Basis of Specificity for Carboxyl-Terminated Acyl Donors in a Bacterial Acyltransferase.,Xiao F, Dong S, Liu Y, Feng Y, Li H, Yun CH, Cui Q, Li W J Am Chem Soc. 2020 Sep 1. doi: 10.1021/jacs.0c07331. PMID:32803979[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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