Literature DB >> 7866749

Structure of the Escherichia coli signal transducing protein PII.

E Cheah1, P D Carr, P M Suffolk, S G Vasudevan, N E Dixon, D L Ollis.   

Abstract

BACKGROUND: In Gram-negative proteobacteria, the nitrogen level in the cell is reflected by the uridylylation status of a key signal transducing protein, PII. PII modulates the activity of glutamine synthetase (GS) through its interaction with adenylyl transferase and it represses the expression of GS by acting in concert with nitrogen regulatory protein II.
RESULTS: The three-dimensional structure of the Escherichia coli PII trimer has been determined at 2.7 A resolution. PII shows a low level of structural similarity to a broad family of alpha/beta proteins and contains a double beta alpha beta motif. The PII trimer contains three beta-sheets, each of which is composed of strands from each of the three monomers. These are surrounded by six alpha-helices.
CONCLUSIONS: The structure of PII suggests potential regions of interaction with other proteins and serves as an initial step in understanding its signal transducing role in nitrogen regulation.

Entities:  

Mesh:

Substances:

Year:  1994        PMID: 7866749     DOI: 10.1016/s0969-2126(94)00100-6

Source DB:  PubMed          Journal:  Structure        ISSN: 0969-2126            Impact factor:   5.006


  30 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.  X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.

Authors:  Alexei Savchenko; Tatiana Skarina; Elena Evdokimova; James D Watson; Roman Laskowski; Cheryl H Arrowsmith; Aled M Edwards; Andrzej Joachimiak; Rong-guang Zhang
Journal:  Proteins       Date:  2004-01-01

3.  Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein.

Authors:  Augen A Pioszak; Alexander J Ninfa
Journal:  J Bacteriol       Date:  2003-02       Impact factor: 3.490

4.  Interpreting the plastid carbon, nitrogen, and energy status. A role for PII?

Authors:  Greg B G Moorhead; Catherine S Smith
Journal:  Plant Physiol       Date:  2003-10       Impact factor: 8.340

5.  Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake.

Authors:  Ozkan Yildiz; Christoph Kalthoff; Stefan Raunser; Werner Kühlbrandt
Journal:  EMBO J       Date:  2007-01-04       Impact factor: 11.598

6.  The 2.2 A resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain.

Authors:  Michael H Godsey; George Minasov; Ludmilla Shuvalova; Joseph S Brunzelle; Ivan I Vorontsov; Frank R Collart; Wayne F Anderson
Journal:  Protein Sci       Date:  2007-07       Impact factor: 6.725

7.  Applying charge discrimination with electrospray ionization-mass spectrometry to protein analyses.

Authors:  J A Loo; R R Ogorzalek Loo
Journal:  J Am Soc Mass Spectrom       Date:  1995-11       Impact factor: 3.109

8.  Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunits.

Authors:  P Jiang; P Zucker; A J Ninfa
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

9.  Expression of glnB and a glnB-like gene (glnK) in a ribulose bisphosphate carboxylase/oxygenase-deficient mutant of Rhodobacter sphaeroides.

Authors:  Y Qian; F R Tabita
Journal:  J Bacteriol       Date:  1998-09       Impact factor: 3.490

10.  Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.

Authors:  Bagautdin Bagautdinov; Yoshinori Matsuura; Svetlana Bagautdinova; Naoki Kunishima; Katsuhide Yutani
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2008-04-30
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.