Literature DB >> 15103149

Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae.

Alan Riboldi-Tunnicliffe1, Marie Claude Trombe, Colin J Bent, Neil W Isaacs, Timothy J Mitchell.   

Abstract

RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N-terminal receiver domain and a C-terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2-234) has been crystallized using the sitting-drop vapour-diffusion technique. The crystals belong to space group P2(1), with unit-cell parameters a = 46.46, b = 32.61, c = 63.35 A, beta = 90.01 degrees. X-ray diffraction data have been collected to 1.93 A resolution.

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Year:  2004        PMID: 15103149     DOI: 10.1107/S0907444904005712

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Discovery of novel inhibitors of Streptococcus pneumoniae based on the virtual screening with the homology-modeled structure of histidine kinase (VicK).

Authors:  Nan Li; Fei Wang; Siqiang Niu; Ju Cao; Kaifeng Wu; Youqiang Li; Nanlin Yin; Xuemei Zhang; Weiliang Zhu; Yibing Yin
Journal:  BMC Microbiol       Date:  2009-06-27       Impact factor: 3.605

  1 in total

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