8yyr
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the HitB T293G mutant== | |
| + | <StructureSection load='8yyr' size='340' side='right'caption='[[8yyr]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8yyr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Embleya_scabrispora Embleya scabrispora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YYR 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1L0H:[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+~{N}-[(3~{S})-3-azanyl-3-(2-bromophenyl)propanoyl]sulfamate'>A1L0H</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=8yyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yyr OCA], [https://pdbe.org/8yyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yyr RCSB], [https://www.ebi.ac.uk/pdbsum/8yyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yyr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0F7R6G7_9ACTN A0A0F7R6G7_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Adenylation enzymes catalyze the selective incorporation of aminoacyl building blocks in the biosynthesis of nonribosomal peptides and related natural products. Although beta-amino acid units are one of the important aminoacyl building blocks in natural product biosynthesis, very little is known about the engineering of beta-amino acid adenylation enzymes. In this study, we engineered the substrate specificity of the (S)-beta-phenylalanine adenylation enzyme, HitB, involved in the biosynthesis of macrolactam polyketide hitachimycin. Based on the previously determined structure of HitB wild-type, we mutated Phe328 and Ser293, which are located near the meta and ortho position of the (S)-beta-phenylalanine moiety, respectively. As a result, the HitB F328V and F328L mutants efficiently activated meta-substituted (S)-beta-phenylalanine analogs, and the HitB T293G and T293S mutants efficiently activated ortho-substituted (S)-beta-phenylalanine analogs. Structural analysis of the HitB F328L and T293G mutants with the corresponding nonhydrolyzable intermediate analogs revealed an enlarged substrate binding pocket for (S)-beta-phenylalanine analogs, providing detailed insights into the structural basis for creating enzyme substrate promiscuity. Our findings may be useful for production of various beta-amino acid-containing natural product analogs. | ||
| - | + | Engineering the Substrate Specificity of (S)-beta-Phenylalanine Adenylation Enzyme HitB.,Wang D, Miyanaga A, Chisuga T, Kudo F, Eguchi T Chembiochem. 2024 May 28:e202400383. doi: 10.1002/cbic.202400383. PMID:38805007<ref>PMID:38805007</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8yyr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Embleya scabrispora]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chisuga T]] | ||
| + | [[Category: Eguchi T]] | ||
| + | [[Category: Kudo F]] | ||
| + | [[Category: Miyanaga A]] | ||
| + | [[Category: Wang D]] | ||
Current revision
Structure of the HitB T293G mutant
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