The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain

Francois-Xavier Chauviac; Giles Robertson; Doris H. X. Quay; Claire Bagneris; Christian Dumas; Brian Henderson; John Ward; Nicholas H. Keep; Martin Cohen-Gonsaud

doi:10.1107/S2053230X1401317X

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The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain

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The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain

Francois-Xavier Chauviac, Giles Robertson, Doris H. X. Quay, Claire Bagneris, Christian Dumas, Brian Henderson, John Ward, Nicholas H. Keep et Martin Cohen-Gonsaud

Acta crystallographica. Section F, Structural biology communications, Vol.70(8), pp.1022-1026

08/2014

DOI: https://doi.org/10.1107/S2053230X1401317X

PMID: 25084374

Résumé

Biochemical Research Methods

Biochemistry & Molecular Biology

Biophysics

Crystallography

Life Sciences & Biomedicine

Physical Sciences

Science & Technology

The first structure of the catalytic domain of RpfC (Rv1884), one of the resuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis, is reported. The structure was solved using molecular replacement once the space group had been correctly identified as twinned P2(1) rather than the apparent C222(1) by searching for anomalous scattering sites in P1. The structure displays a very high degree of structural conservation with the previously published structures of the catalytic domains of RpfB (Rv1009) and RpfE (Rv2450). This structural conservation highlights the importance of the versatile domain composition of the RPF family.

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Titre: The RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation-promoting factor catalytic domain
Créateurs - sans rôle: Francois-Xavier Chauviac - Univ London, Inst Struct & Mol Biol, Dept Biol Sci, London WC1E 7HX, England
Giles Robertson - Univ London, Inst Struct & Mol Biol, Dept Biol Sci, London WC1E 7HX, England
Doris H. X. Quay - Univ London, Inst Struct & Mol Biol, Dept Biol Sci, London WC1E 7HX, England
Claire Bagneris - University of London
Christian Dumas - CNRS, Ctr Biochim Struct, UMR 5048, F-34090 Montpellier, France
Brian Henderson - UCL, UCL Eastman Dent Inst, Dept Microbial Dis, London WC1X 8LD, England
John Ward - UCL, Dept Biochem Engn, Adv Ctr Biochem Engn, London WC1E 7JE, England
Nicholas H. Keep - University of London
Martin Cohen-Gonsaud - Univ London, Inst Struct & Mol Biol, Dept Biol Sci, London WC1E 7HX, England
Détails de publication: Acta crystallographica. Section F, Structural biology communications, Vol.70(8), pp.1022-1026
Éditeur: Int Union Crystallography
Nombre de pages: 5
Note de subvention: BB/F011148/1 / Biotechnology and Biological Sciences Research Council; UK Research & Innovation (UKRI); Biotechnology and Biological Sciences Research Council (BBSRC) G0401038 / Medical Research Council; UK Research & Innovation (UKRI); Medical Research Council UK (MRC); European Commission MYCS-2011-252 / Commonwealth Studies Commission studentship BB/F011148/1 / BBSRC; UK Research & Innovation (UKRI); Biotechnology and Biological Sciences Research Council (BBSRC) ANR-10-INSB-05-01 / French Infrastructure for Integrated Structural Biology (FRISBI) X-TB Struct EU grant Bloomsbury studentship G0401038 / MRC; UK Research & Innovation (UKRI); Medical Research Council UK (MRC)
Identifiants: 99136067509311
Unité académique: Centre de Biologie Structurale - CBS
Langue: English
Type de ressource: Journal article