9s3l: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "9s3l" [edit=sysop:move=sysop] |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==ClxA from Clostridium cavendishii (apo)== | ||
<StructureSection load='9s3l' size='340' side='right'caption='[[9s3l]], [[Resolution|resolution]] 2.57Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9s3l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium Clostridium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S3L FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9s3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s3l OCA], [https://pdbe.org/9s3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s3l RCSB], [https://www.ebi.ac.uk/pdbsum/9s3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s3l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1M6IZB6_9CLOT A0A1M6IZB6_9CLOT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The synthesis of ester bonds using lipases is one of the most frequently performed reactions in biocatalysis, yet examples of the enzymatic synthesis of phenyl benzoate esters are comparatively rare. In this report we show that the ligase ClxA, from Clostridium cavendishii, initially reported to have roles in amide bond formation in the biosynthesis of benzoxazole antibiotics, is an effective catalyst for the formation of phenyl benzoate esters from acid and phenol substrates using ATP in an aqueous medium. The structure of ClxA in a complex with both AMP and 3,4-aminohydroxybenzoic acid was determined by X-ray crystallography to 2.15 A resolution and used as a platform to engineer the enzyme to create variants N226L and K140A possessing broader substrate specificity for ester formation, and also the ability to enable the synthesis of native amide product oligomers. | |||
Biocatalytic synthesis of phenyl benzoate esters using the amide ligase ClxA.,Ascham A, Tang Q, Fairlamb IJS, Grogan G RSC Chem Biol. 2025 Oct 8. doi: 10.1039/d5cb00205b. PMID:41098411<ref>PMID:41098411</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Ascham | <div class="pdbe-citations 9s3l" style="background-color:#fffaf0;"></div> | ||
[[Category: Grogan | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium]] | |||
[[Category: Large Structures]] | |||
[[Category: Ascham A]] | |||
[[Category: Grogan G]] | |||
Latest revision as of 07:51, 19 November 2025
ClxA from Clostridium cavendishii (apo)
| ||||||||||||
