7y4h

</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=7y4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y4h OCA], [https://pdbe.org/7y4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y4h RCSB], [https://www.ebi.ac.uk/pdbsum/7y4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y4h ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Identifying new environmental resistance determinants is significant to combat rising antibiotic resistance. Herein we report the unexpected correlation of a lobophorin (LOB) resistance-related glycosidase KijX with the host-dependent chemical diversity of LOBs, by a process of glycosylation, deglycosylation and reglycosylation. KijX homologues are widespread among bacteria, archaea and fungi, and encode the same glycohydrolytic activity on LOBs. The crystal structure of AcvX (a KijX homologue) shows a similar fold to that of the glycoside hydrolase family 113 and a special negatively charged groove to accommodate and deglycosylate LOBs. Antagonistic assays indicate kijX as a defense weapon of actinomycetes to combat LOB producers in environment, reflecting an elegant coevolution relationship. Our study provides insight into the KijX-related glycosidases as preexisting resistance determinants and represents an example of resistance genes accidentally integrated into natural product assembly.

A Widespread Glycosidase Confers Lobophorin Resistance and Host-Dependent Structural Diversity.,Tan B, Zhang L, Zhang Q, Chen S, Xiong W, Zhu Y, Zhang C Angew Chem Int Ed Engl. 2023 Apr 19:e202302043. doi: 10.1002/anie.202302043. PMID:37076762<ref>PMID:37076762</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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