Literature DB >> 16682779

Crystallization and preliminary X-ray analysis of CooA from Carboxydothermus hydrogenoformans.

Hirofumi Komori1, Kensuke Satomoto, Yasufumi Ueda, Naoki Shibata, Sayaka Inagaki, Shiro Yoshioka, Shigetoshi Aono, Yoshiki Higuchi.   

Abstract

CooA, a homodimeric haem-containing protein, is responsible for transcriptional regulation in response to carbon monoxide (CO). It has a b-type haem as a CO sensor. Upon binding CO to the haem, CooA binds promoter DNA and activates expression of genes for CO metabolism. CooA from Carboxydothermus hydrogenoformans has been overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method. The crystal belongs to space group P2(1), with unit-cell parameters a = 61.8, b = 94.7, c = 92.8 angstroms, beta = 104.8 degrees. The native and anomalous difference Patterson maps indicated that two CooA dimers are contained in the asymmetric unit and are related by a translational symmetry almost parallel to the c axis.

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Year:  2006        PMID: 16682779      PMCID: PMC2219970          DOI: 10.1107/S1744309106012826

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


  10 in total

1.  The finer things in X-ray diffraction data collection.

Authors:  J W Pflugrath
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1999-10

2.  Structure of the CO sensing transcription activator CooA.

Authors:  W N Lanzilotta; D J Schuller; M V Thorsteinsson; R L Kerby; G P Roberts; T L Poulos
Journal:  Nat Struct Biol       Date:  2000-10

Review 3.  Transcription activation by catabolite activator protein (CAP).

Authors:  S Busby; R H Ebright
Journal:  J Mol Biol       Date:  1999-10-22       Impact factor: 5.469

4.  CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein.

Authors:  D Shelver; R L Kerby; Y He; G P Roberts
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-14       Impact factor: 11.205

5.  A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum.

Authors:  S Aono; H Nakajima; K Saito; M Okada
Journal:  Biochem Biophys Res Commun       Date:  1996-11-21       Impact factor: 3.575

6.  Solvent content of protein crystals.

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

7.  Spectroscopic and redox properties of a CooA homologue from Carboxydothermus hydrogenoformans.

Authors:  Sayaka Inagaki; Chiaki Masuda; Tetsuhiro Akaishi; Hiroshi Nakajima; Shiro Yoshioka; Takehiro Ohta; Biswajit Pal; Teizo Kitagawa; Shigetoshi Aono
Journal:  J Biol Chem       Date:  2004-11-10       Impact factor: 5.157

8.  Functionally critical elements of CooA-related CO sensors.

Authors:  Hwan Youn; Robert L Kerby; Mary Conrad; Gary P Roberts
Journal:  J Bacteriol       Date:  2004-03       Impact factor: 3.490

9.  Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees.

Authors:  S C Schultz; G C Shields; T A Steitz
Journal:  Science       Date:  1991-08-30       Impact factor: 47.728

10.  Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

Authors:  D B McKay; T A Steitz
Journal:  Nature       Date:  1981-04-30       Impact factor: 49.962

  10 in total
  1 in total

1.  Interactions and dynamics of the Shine Dalgarno helix in the 70S ribosome.

Authors:  Andrei Korostelev; Sergei Trakhanov; Haruichi Asahara; Martin Laurberg; Laura Lancaster; Harry F Noller
Journal:  Proc Natl Acad Sci U S A       Date:  2007-10-16       Impact factor: 11.205

  1 in total

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