Literature DB >> 7966297

Preliminary X-ray diffraction analysis of crystals of the PII protein from Escherichia coli.

V S de Mel1, E S Kamberov, P D Martin, J Zhang, A J Ninfa, B F Edwards.   

Abstract

PII protein, which carries metabolic signals regulating the transcription and activity of glutamine synthetase in nitrogen assimilation in Escherichia coli, has been crystallized in space group P2(1) with a = 47.8 A, b = 62.9 A, c = 52.8 A and beta = 100.3 degrees and space group P2(1)2(1)2(1) with a = 52.2 A. b = 64.9 A and c = 100.1 A. Both the monoclinic crystals, which diffract beyond 3.0 A, and the orthorhombic crystals, which diffract beyond 2.5 A, probably have three molecules of 12,400 Da each in the crystallographic asymmetric unit.

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Year:  1994        PMID: 7966297     DOI: 10.1016/0022-2836(94)90049-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  4 in total

Review 1.  P(II) signal transduction proteins, pivotal players in microbial nitrogen control.

Authors:  T Arcondéguy; R Jack; M Merrick
Journal:  Microbiol Mol Biol Rev       Date:  2001-03       Impact factor: 11.056

2.  Characterization of the glnK-amtB operon of Azotobacter vinelandii.

Authors:  D Meletzus; P Rudnick; N Doetsch; A Green; C Kennedy
Journal:  J Bacteriol       Date:  1998-06       Impact factor: 3.490

Review 3.  Nitrogen control in bacteria.

Authors:  M J Merrick; R A Edwards
Journal:  Microbiol Rev       Date:  1995-12

Review 4.  Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.

Authors:  Wally C van Heeswijk; Hans V Westerhoff; Fred C Boogerd
Journal:  Microbiol Mol Biol Rev       Date:  2013-12       Impact factor: 11.056

  4 in total

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