9uay: Difference between revisions

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'''Unreleased structure'''


The entry 9uay is ON HOLD  until Paper Publication
==Crystal structure of CmnI==
<StructureSection load='9uay' size='340' side='right'caption='[[9uay]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9uay]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharothrix_mutabilis_subsp._capreolus Saccharothrix mutabilis subsp. capreolus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UAY 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]] 2.17&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=AE4:3,6,9,12,15-PENTAOXAHEPTADECAN-1-OL'>AE4</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=9uay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9uay OCA], [https://pdbe.org/9uay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9uay RCSB], [https://www.ebi.ac.uk/pdbsum/9uay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9uay ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Capreomycin (CMN) is a nonribosomal peptide (NRP) antituberculosis antibiotic. CMN biosynthesis involves a non-canonical trans-iterative adenylation (A) domain. Here, we report that the A domain-less nonribosomal peptide synthetase (NRPS) module CmnI utilizes another module's A domain CmnA-A(1) to load the required amino acid onto its thiolation (T) domain. This study provides evidence of an unusual mode of NRP biosynthesis in bacteria, involving a trans-iterative A domain in the NRPS machinery.


Authors: Hsiao, P.Y., Chang, C.Y., Peng, C.Y.
Biosynthesis of Antituberculosis Antibiotic Capreomycin Involves a trans-Iterative Adenylation Domain within the Nonribosomal Peptide Synthetase Machinery.,Lai YT, Peng CY, Liao HT, Hsiao PY, Hsieh CK, Luo YR, Huang SC, Wang YL, Ma T, Chen YR, Kuo YM, Lin YC, Chu J, Chang CY Org Lett. 2025 Aug 29;27(34):9553-9558. doi: 10.1021/acs.orglett.5c03112. Epub , 2025 Aug 15. PMID:40815678<ref>PMID:40815678</ref>


Description: Crystal structure of CmnI
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Chang, C.Y]]
<div class="pdbe-citations 9uay" style="background-color:#fffaf0;"></div>
[[Category: Peng, C.Y]]
== References ==
[[Category: Hsiao, P.Y]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharothrix mutabilis subsp. capreolus]]
[[Category: Chang CY]]
[[Category: Hsiao PY]]
[[Category: Peng CY]]