Literature DB >> 20383012

Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv.

Bernhard Sielaff1, Ki Seog Lee, Francis T F Tsai.   

Abstract

Full-length GroEL1 from Mycobacterium tuberculosis H37Rv was cloned, overexpressed and purified. Crystals were obtained by the hanging-drop vapor-diffusion method and contained a 23 kDa GroEL1 fragment. A complete native data set was collected from a single frozen crystal that belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 75.47, b = 78.67, c = 34.89 A, alpha = beta = gamma = 90 degrees , and diffracted to 2.2 A resolution on a home X-ray source.

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Year:  2010        PMID: 20383012      PMCID: PMC2852334          DOI: 10.1107/S1744309110004409

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


  15 in total

1.  Identification of in vivo substrates of the chaperonin GroEL.

Authors:  W A Houry; D Frishman; C Eckerskorn; F Lottspeich; F U Hartl
Journal:  Nature       Date:  1999-11-11       Impact factor: 49.962

2.  Crystal structure of wild-type chaperonin GroEL.

Authors:  Cecilia Bartolucci; Doriano Lamba; Saulius Grazulis; Elena Manakova; Hermann Heumann
Journal:  J Mol Biol       Date:  2005-10-21       Impact factor: 5.469

3.  The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.

Authors:  Z Xu; A L Horwich; P B Sigler
Journal:  Nature       Date:  1997-08-21       Impact factor: 49.962

4.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

5.  Heat shock proteome analysis of wild-type Corynebacterium glutamicum ATCC 13032 and a spontaneous mutant lacking GroEL1, a dispensable chaperone.

Authors:  Carlos Barreiro; Eva González-Lavado; Sven Brand; Andreas Tauch; Juan F Martín
Journal:  J Bacteriol       Date:  2005-02       Impact factor: 3.490

6.  The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures.

Authors:  O Fayet; T Ziegelhoffer; C Georgopoulos
Journal:  J Bacteriol       Date:  1989-03       Impact factor: 3.490

7.  Mycobacterium tuberculosis expresses two chaperonin-60 homologs.

Authors:  T H Kong; A R Coates; P D Butcher; C J Hickman; T M Shinnick
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-01       Impact factor: 11.205

8.  Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays.

Authors:  Graham R Stewart; Lorenz Wernisch; Richard Stabler; Joseph A Mangan; Jason Hinds; Ken G Laing; Douglas B Young; Philip D Butcher
Journal:  Microbiology       Date:  2002-10       Impact factor: 2.777

Review 9.  Multiple chaperonins in bacteria--why so many?

Authors:  Peter A Lund
Journal:  FEMS Microbiol Rev       Date:  2009-04-07       Impact factor: 16.408

10.  A novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroEL.

Authors:  Debashree Basu; Garima Khare; Shashi Singh; Anil Tyagi; Sanjeev Khosla; Shekhar C Mande
Journal:  Nucleic Acids Res       Date:  2009-06-15       Impact factor: 16.971

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  3 in total

1.  Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.

Authors:  Bernhard Sielaff; Ki Seog Lee; Francis T F Tsai
Journal:  J Mol Biol       Date:  2010-11-19       Impact factor: 5.469

Review 2.  Multiple chaperonins in bacteria--novel functions and non-canonical behaviors.

Authors:  C M Santosh Kumar; Shekhar C Mande; Gaurang Mahajan
Journal:  Cell Stress Chaperones       Date:  2015-05-20       Impact factor: 3.667

3.  Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.

Authors:  Juliane Winkler; Jens Tyedmers; Bernd Bukau; Axel Mogk
Journal:  J Cell Biol       Date:  2012-08-06       Impact factor: 10.539

  3 in total

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