Literature DB >> 18391418

Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.

Jingshan Ren1, Joanne E Nettleship, Sarah Sainsbury, Nigel J Saunders, Raymond J Owens.   

Abstract

The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM.

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Year:  2008        PMID： 18391418      PMCID： PMC2374261          DOI： 10.1107/S1744309108005411

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


  27 in total

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Authors:  W Kremer; B Schuler; S Harrieder; M Geyer; W Gronwald; C Welker; R Jaenicke; H R Kalbitzer
Journal:  Eur J Biochem       Date:  2001-05

2.  Escherichia coli CspA-family RNA chaperones are transcription antiterminators.

Authors:  W Bae; B Xia; M Inouye; K Severinov
Journal:  Proc Natl Acad Sci U S A       Date:  2000-07-05       Impact factor: 11.205

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4.  Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.

Authors:  Markus Zeeb; Jochen Balbach
Journal:  Protein Sci       Date:  2003-01       Impact factor: 6.725

5.  Improved methods for building protein models in electron density maps and the location of errors in these models.

Authors:  T A Jones; J Y Zou; S W Cowan; M Kjeldgaard
Journal:  Acta Crystallogr A       Date:  1991-03-01       Impact factor: 2.290

6.  RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain.

Authors:  D Landsman
Journal:  Nucleic Acids Res       Date:  1992-06-11       Impact factor: 16.971

7.  Complete genome sequence of Neisseria meningitidis serogroup B strain MC58.

Authors:  H Tettelin; N J Saunders; J Heidelberg; A C Jeffries; K E Nelson; J A Eisen; K A Ketchum; D W Hood; J F Peden; R J Dodson; W C Nelson; M L Gwinn; R DeBoy; J D Peterson; E K Hickey; D H Haft; S L Salzberg; O White; R D Fleischmann; B A Dougherty; T Mason; A Ciecko; D S Parksey; E Blair; H Cittone; E B Clark; M D Cotton; T R Utterback; H Khouri; H Qin; J Vamathevan; J Gill; V Scarlato; V Masignani; M Pizza; G Grandi; L Sun; H O Smith; C M Fraser; E R Moxon; R Rappuoli; J C Venter
Journal:  Science       Date:  2000-03-10       Impact factor: 47.728

8.  Structure in solution of the major cold-shock protein from Bacillus subtilis.

Authors:  A Schnuchel; R Wiltscheck; M Czisch; M Herrler; G Willimsky; P Graumann; M A Marahiel; T A Holak
Journal:  Nature       Date:  1993-07-08       Impact factor: 49.962

9.  Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.

Authors:  K Newkirk; W Feng; W Jiang; R Tejero; S D Emerson; M Inouye; G T Montelione
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-24       Impact factor: 11.205

10.  Maximum-likelihood density modification.

Authors:  T C Terwilliger
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2000-08
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  3 in total

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2.  Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.

Authors:  Alonso I Carvajal; Gabriel Vallejos; Elizabeth A Komives; Víctor Castro-Fernández; Diego A Leonardo; Richard C Garratt; César A Ramírez-Sarmiento; Jorge Babul
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Review 3.  β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.

Authors:  Anna I Sulatskaya; Anastasiia O Kosolapova; Alexander G Bobylev; Mikhail V Belousov; Kirill S Antonets; Maksim I Sulatsky; Irina M Kuznetsova; Konstantin K Turoverov; Olesya V Stepanenko; Anton A Nizhnikov
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