View source for 9lmm


==An antibiotic biosynthesis monooxygenase family protein from Streptomyces sp. MA37==
<StructureSection load='9lmm' size='340' side='right'caption='[[9lmm]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9lmm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._MA37 Streptomyces sp. MA37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LMM 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]] 1.65&#8491;</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=9lmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lmm OCA], [https://pdbe.org/9lmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lmm RCSB], [https://www.ebi.ac.uk/pdbsum/9lmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lmm ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9lmm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. MA37]]
[[Category: Jiang K]]
[[Category: Qu XD]]