Literature DB >> 21370306

Crystal structure of calcium dodecin (Rv0379), from Mycobacterium tuberculosis with a unique calcium-binding site.

Arulandu Arockiasamy1, Anup Aggarwal, Christos G Savva, Andreas Holzenburg, James C Sacchettini.   

Abstract

In eukaryotes, calcium-binding proteins play a pivotal role in diverse cellular processes, and recent findings suggest similar roles for bacterial proteins at different stages in their life cycle. Here, we report the crystal structure of calcium dodecin, Rv0379, from Mycobacterium tuberculosis with a dodecameric oligomeric assembly and a unique calcium-binding motif. Structure and sequence analysis were used to identify orthologs of Rv0379 with different ligand-binding specificity.
Copyright © 2011 The Protein Society.

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Year:  2011        PMID: 21370306      PMCID: PMC3125867          DOI: 10.1002/pro.607

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  35 in total

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Review 3.  Annexins: linking Ca2+ signalling to membrane dynamics.

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Journal:  Proc Natl Acad Sci U S A       Date:  2004-10-28       Impact factor: 11.205

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7.  The dodecin from Thermus thermophilus, a bifunctional cofactor storage protein.

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8.  Dodecin is the key player in flavin homeostasis of archaea.

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Review 9.  XtalView, protein structure solution and protein graphics, a short history.

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10.  Calcium signalling in Bacillus subtilis.

Authors:  M L Herbaud; A Guiseppi; F Denizot; J Haiech; M C Kilhoffer
Journal:  Biochim Biophys Acta       Date:  1998-12-10
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  1 in total

Review 1.  Interrelation of Ca2+ and PE_PGRS proteins during Mycobacterium tuberculosis pathogenesis.

Authors:  Laxman S Meena
Journal:  J Biosci       Date:  2019-03       Impact factor: 1.826

  1 in total

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