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dc.contributor.authorXiong, Junhui
dc.contributor.authorYang, Chunyan
dc.contributor.authorGe, Shengxiang
dc.contributor.authorLi, Shaowei
dc.contributor.authorXia, Ningshao
dc.contributor.author夏宁绍
dc.contributor.authorLiu, Fengxia ( Natl Univ Singapore)
dc.contributor.authorKumar, Sundaramurthy ( Natl Univ Singapore)
dc.contributor.authorSwaminathan, Kunchithapadam ( Natl Univ Singapore)
dc.date.accessioned2012-07-28T09:15:48Z
dc.date.available2012-07-28T09:15:48Z
dc.date.issued2011-04-24
dc.identifier.citationJournal of Structural Biology Volume 175, Issue 1, July 2011, Pages 31–38zh_CN
dc.identifier.issn1047-8477
dc.identifier.urihttp://dx.doi.org/doi:10.1016/j.jsb.2011.04.013
dc.identifier.uriWOS:000291371800004
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/13360
dc.description.abstractDodecins (assembly of twelve monomers) are the smallest known flavoprotein with only 65-73 amino acids and are involved in binding and storage of flavins in archaea. Here we report the crystal structure of Rv1498A, a Mycobacterium tuberculosis dodecin. This bacterial dodecin structure is similar to that of other reported dodecins. Each monomer has a 3 stranded beta-sheet and an alpha-helix perpendicular to it. This protein has polyextreme (halophilic and thermophilic) properties. Interestingly, positively and negatively charged residues aggregate separately and do not seem to contribute to thermophilic and halophilic stability. We have examined the interactions that stabilize the Rv1498A dodecamer by preparing selected point mutants that break salt bridges and hydrophobic contacts, thereby leading to collapse of the assembly. (C) 2011 Elsevier Inc. All rights reserved.zh_CN
dc.description.sponsorshipNational University of Singapore (NUS)/Singapore Ministry of Educatio; Singapore Biomedical Research Council (BMRC); Life Science Institute of NUS; National Natural Science Foundation for Distinguished Young Scholars[30925030]; Project 863[2006AA020905]; Project 111[B06016]; Key Program in Infectious Diseases of the People's Republic of China[2008ZX10002-012, 2009ZX09102]; BMRCzh_CN
dc.language.isoenzh_CN
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCEzh_CN
dc.subjectMycobacterium tuberculosiszh_CN
dc.subjectDodecinzh_CN
dc.subjectX-ray crystallographyzh_CN
dc.subjectAssemblyzh_CN
dc.subjectPolyextremezh_CN
dc.titleStructural and biophysical characterization of Mycobacterium tuberculosis dodecin Rv1498Azh_CN
dc.typeArticlezh_CN


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