9lmn

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Current revision (06:26, 26 November 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9lmn is ON HOLD until Paper Publication
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==Crystal structure of a polyketide ABM/SchA-like domain-containing protein WhiE-ORFI from Streptomyces coelicolor==
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<StructureSection load='9lmn' size='340' side='right'caption='[[9lmn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9lmn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LMN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9lmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lmn OCA], [https://pdbe.org/9lmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lmn RCSB], [https://www.ebi.ac.uk/pdbsum/9lmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lmn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/WH42_STRCO WH42_STRCO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aromatic polyketides are a vast category of natural products known for their wide-ranging biological activities, with their structural variety stemming from modifications to their core frameworks. This study reveals two distinct processes that shape the frameworks of (+)/(-)-anthrabenzoxocinone (ABX) and fasamycin (FAS) from a common biosynthetic precursor, compound 1. FasS protects the carboxyl group of this molecule without altering it, preparing it for FasU, which then crafts FAS's unique, nonplanar axial chiral aromatic framework. In contrast, Abx((+))O and Abx((-))O remove the carboxyl group from compound 1, producing phenyldimethylanthrone (PDA), a key intermediate for (+)/(-)-ABX formation. Structural analysis of AccS (1.65 A, FasS homologue) and Abx((+))O (1.99 A), combined with mutagenesis studies, identifies key residues of AccS and Abx((+))O, providing insights into the carboxyl-protecting mechanism and decarboxylation mechanism. Evolutionary and functional studies further connect AccS and AbxO to the N- and C-termini of the long-studied, functionally enigmatic protein family, WhiE-ORFI (resolved in 2.3 A). This study unveils hidden strategies for terminal carboxyl group editing, providing new insights into the origins of aromatic polyketide diversity.
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Authors:
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Terminal Carboxyl Editing Drives Divergence in Fasamycin and Anthrabenzoxocinone Biosynthesis.,Jiang K, Zhu C, Gao Y, Dai Y, Yan X, Yang L, Jiang M, Lin Z, Deng Z, Luo S, Qu X J Am Chem Soc. 2025 Jul 30;147(30):26468-26476. doi: 10.1021/jacs.5c06089. Epub , 2025 Jul 21. PMID:40690660<ref>PMID:40690660</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9lmn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Jiang K]]
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[[Category: Qu XD]]

Current revision

Crystal structure of a polyketide ABM/SchA-like domain-containing protein WhiE-ORFI from Streptomyces coelicolor

PDB ID 9lmn

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