Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/94013
DC FieldValueLanguage
dc.contributor.authorChen, Sheng-Chiazh_TW
dc.contributor.authorHuang, Chi-Hungzh_TW
dc.contributor.authorLai, Shu-Jungzh_TW
dc.contributor.authorLiu, Jai-Shinzh_TW
dc.contributor.authorFu, Pin-Kueizh_TW
dc.contributor.authorTseng, Shih-Tingzh_TW
dc.contributor.authorYang, Chia Shinzh_TW
dc.contributor.authorLai, Mei-Chinzh_TW
dc.contributor.authorKo, Tzu-Pingzh_TW
dc.contributor.authorChen, Yehzh_TW
dc.date2015-
dc.date.accessioned2016-08-08T06:49:10Z-
dc.date.available2016-08-08T06:49:10Z-
dc.identifier.urihttp://hdl.handle.net/11455/94013-
dc.description.abstractStreptosporangium sibiricum SibL catalyzes the methyl transfer from S-adenosylmethionine (SAM) to 3-hydroxykynurenine (3-HK) to produce S-adenosylhomocysteine (SAH) and 3-hydroxy-4-methyl-kynurenine for sibiromycin biosynthesis. Here, we present the crystal structures of apo-form Ss-SibL, Ss-SibL/SAH binary complex and Ss-SibL/SAH/3-HK ternary complex. Ss-SibL is a homodimer. Each subunit comprises a helical N-terminal domain and a Rossmann-fold C-terminal domain. SAM (or SAH) binding alone results in domain movements, suggesting a two-step catalytic cycle. Analyses of the enzyme-ligand interactions and further mutant studies support a mechanism in which Tyr134 serves as the principal base in the transferase reaction of methyl group from SAM to 3-HK.zh_TW
dc.language.isoenzh_TW
dc.relationScientific reports, Volume 5, Page(s) 10100.zh_TW
dc.subjectActinobacteriazh_TW
dc.subjectAnti-Bacterial Agentszh_TW
dc.subjectBacterial Proteinszh_TW
dc.subjectBinding Siteszh_TW
dc.subjectCrystallography, X-Rayzh_TW
dc.subjectKynureninezh_TW
dc.subjectLigandszh_TW
dc.subjectMethyltransferaseszh_TW
dc.subjectModels, Molecularzh_TW
dc.subjectMutant Proteinszh_TW
dc.subjectProtein Multimerizationzh_TW
dc.subjectProtein Structure, Secondaryzh_TW
dc.titleStructure and mechanism of an antibiotics-synthesizing 3-hydroxykynurenine C-methyltransferasezh_TW
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1038/srep10100zh_TW
item.grantfulltextnone-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
Appears in Collections:生命科學系所
Show simple item record
 

Google ScholarTM

Check

Altmetric

Altmetric


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