Open Access System for Information Sharing

Login Library

 

Article
Cited 3 time in webofscience Cited 3 time in scopus
Metadata Downloads
Full metadata record
Files in This Item:
There are no files associated with this item.
DC FieldValueLanguage
dc.contributor.authorChung, Scisung-
dc.contributor.authorKim, Sulhee-
dc.contributor.authorRyu, Sung Ho-
dc.contributor.authorHwang, Kwang Yeon-
dc.contributor.authorCho, Yunje-
dc.date.accessioned2021-12-03T09:43:39Z-
dc.date.available2021-12-03T09:43:39Z-
dc.date.created2020-05-21-
dc.date.issued2020-04-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oasis.postech.ac.kr/handle/2014.oak/107903-
dc.description.abstractPathogenic aminoacyl-tRNA synthetases (ARSs) are attractive targets for anti-infective agents because their catalytic active sites are different from those of human ARSs. Mupirocin is a topical antibiotic that specifically inhibits bacterial isoleucyl-tRNA synthetase (IleRS), resulting in a block to protein synthesis. Previous studies on Thermus thermophilus IleRS indicated that mupirocin-resistance of eukaryotic IleRS is primarily due to differences in two amino acids, His581 and Leu583, in the active site. However, without a eukaryotic IleRS structure, the structural basis for mupirocin-resistance of eukaryotic IleRS remains elusive. Herein, we determined the crystal structure of Candida albicans IleRS complexed with Ile-AMP at 2.9 A resolution. The largest difference between eukaryotic and prokaryotic IleRS enzymes is closure of the active site pocket by Phe55 in the HIGH loop; Arg410 in the CP core loop; and the second Lys in the KMSKR loop. The Ile-AMP product is lodged in a closed active site, which may restrict its release and thereby enhance catalytic efficiency. The compact active site also prevents the optimal positioning of the 9-hydroxynonanoic acid of mupirocin and plays a critical role in resistance of eukaryotic IleRS to anti-infective agents.-
dc.languageEnglish-
dc.publisherKOREAN SOC MOLECULAR & CELLULAR BIOLOGY-
dc.relation.isPartOfMOLECULES AND CELLS-
dc.titleStructural Basis for the Antibiotic Resistance Eukaryotic Isoleucyl-tRNA Synthetase-
dc.typeArticle-
dc.identifier.doi10.14348/molcells.2020.2287-
dc.type.rimsART-
dc.identifier.bibliographicCitationMOLECULES AND CELLS, v.43, no.4, pp.350 - 359-
dc.identifier.wosid000528946600005-
dc.citation.endPage359-
dc.citation.number4-
dc.citation.startPage350-
dc.citation.titleMOLECULES AND CELLS-
dc.citation.volume43-
dc.contributor.affiliatedAuthorChung, Scisung-
dc.contributor.affiliatedAuthorRyu, Sung Ho-
dc.contributor.affiliatedAuthorCho, Yunje-
dc.identifier.scopusid2-s2.0-85084026503-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.type.docTypeArticle-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusPSEUDOMONIC ACID-
dc.subject.keywordPlusRECOGNITION-
dc.subject.keywordPlusADENYLATE-
dc.subject.keywordPlusMUPIROCIN-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusMODEL-
dc.subject.keywordAuthoractive site closure-
dc.subject.keywordAuthoraminoacyl-tRNA synthetases-
dc.subject.keywordAuthoranti-infective agents-
dc.subject.keywordAuthorcrystal structure-
dc.subject.keywordAuthormupirocin-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaCell Biology-

qr_code

  • mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher

류성호RYU, SUNG HO
Dept of Life Sciences
Read more

Views & Downloads

Browse