Literature DB >> 16511148

Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis.

Harriet A Watkins1, MinMin Yu, Edward N Baker.   

Abstract

The Mycobacterium tuberculosis open reading frame Rv3214, annotated as a cofactor-dependent phosphoglycerate mutase, has been cloned and expressed as an N-terminally His-tagged protein. Tagged, untagged and selenomethionine-labelled forms of Rv3214 (EntD) have been purified using nickel-affinity chromatography and gel filtration. The selenomethionine-labelled crystals diffracted to 2.15 A resolution and belong to space group P2(1), with unit-cell parameters a = 44.36, b = 79.03, c = 52.85 A, beta = 109.11 degrees. There are two molecules of molecular weight 21,948 Da per asymmetric unit.

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Year:  2005        PMID： 16511148      PMCID： PMC1952354          DOI： 10.1107/S1744309105020646

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  11 in total

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Journal:  Protein Sci       Date:  2001-09       Impact factor: 6.725

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Authors:  F William Studier
Journal:  Protein Expr Purif       Date:  2005-05       Impact factor: 1.650

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  2 in total

1.  Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.

Authors:  Harriet A Watkins; Edward N Baker
Journal:  J Bacteriol       Date:  2006-05       Impact factor: 3.490

2.  Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.

Authors:  Uday Ganapathy; Joeli Marrero; Susannah Calhoun; Hyungjin Eoh; Luiz Pedro Sorio de Carvalho; Kyu Rhee; Sabine Ehrt
Journal:  Nat Commun       Date:  2015-08-10       Impact factor: 14.919
  2 in total

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