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PDBsum entry 2pii
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Signal transduction protein PDB id
2pii

 

 

 

 

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Contents
Protein chain
112 a.a. *
Waters ×312
* Residue conservation analysis
PDB id:
2pii
Name: Signal transduction protein
Title: Pii, glnb product
Structure: Pii. Chain: a. Synonym: glnb product. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: derived from k12. Variant: an1459. Gene: glnb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.132    
Authors: P.D.Carr,E.Cheah,P.M.Suffolk,D.L.Ollis
Key ref:
P.D.Carr et al. (1996). X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A. Acta Crystallogr D Biol Crystallogr, 52, 93. PubMed id: 15299730 DOI: 10.1107/S0907444995007293
Date:
02-May-95     Release date:   20-Jun-96    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A9Z1  (GLNB_ECOLI) -  Nitrogen regulatory protein P-II 1 from Escherichia coli (strain K12)
Seq:
Struc: 		112 a.a.
112 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1107/S0907444995007293 Acta Crystallogr D Biol Crystallogr 52:93 (1996)
PubMed id: 15299730  
 
 
X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.
P.D.Carr, E.Cheah, P.M.Suffolk, S.G.Vasudevan, N.E.Dixon, D.L.Ollis.
 
  ABSTRACT  
 
The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. MOLSCRIPT (Kraulis. 1991) schematic diagrams of the Pll monomer. (a) Present 1.9 ~ model. (b) Former 2.7~ model. 		Figure 6.
Fig. 6. Secondary structre and hydrogen bonding withn the Pit monomer. This diagram was prepared using the program HERA (Hutchinson & Thornton, 990).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 93-0) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21265784 L.Pedro-Roig, M.Camacho, and M.J.Bonete (2011).
In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei.
  Biochem Soc Trans, 39, 259-262.  
19884192 A.Bandyopadhyay, A.Arora, S.Jain, A.Laskar, C.Mandal, V.A.Ivanisenko, E.S.Fomin, S.S.Pintus, N.A.Kolchanov, S.Maiti, and S.Ramachandran (2010).
Expression and molecular characterization of the Mycobacterium tuberculosis PII protein.
  J Biochem, 147, 279-289.  
20521335 N.D.Shetty, M.C.Reddy, S.K.Palaninathan, J.L.Owen, and J.C.Sacchettini (2010).
Crystal structures of the apo and ATP bound Mycobacterium tuberculosis nitrogen regulatory PII protein.
  Protein Sci, 19, 1513-1524.
PDB codes: 3bzq 3lf0
  18453701 B.Bagautdinov, Y.Matsuura, S.Bagautdinova, N.Kunishima, and K.Yutani (2008).
Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 351-357.
PDB code: 2zfh
19093078 Y.Zhang, and J.Zhao (2008).
PII, the key regulator of nitrogen metabolism in the cyanobacteria.
  Sci China C Life Sci, 51, 1056-1065.  
17506680 J.A.Leigh, and J.A.Dodsworth (2007).
Nitrogen regulation in bacteria and archaea.
  Annu Rev Microbiol, 61, 349-377.  
16864585 A.Durand, and M.Merrick (2006).
In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate.
  J Biol Chem, 281, 29558-29567.  
12949080 F.Arnesano, L.Banci, M.Benvenuti, I.Bertini, V.Calderone, S.Mangani, and M.S.Viezzoli (2003).
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.
  J Biol Chem, 278, 45999-46006.
PDB codes: 1naq 1osc
12084071 E.Machado Benelli, M.Buck, I.Polikarpov, E.Maltempi de Souza, L.M.Cruz, and F.O.Pedrosa (2002).
Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK.
  Eur J Biochem, 269, 3296-3303.
PDB code: 1hwu
11847102 G.Coutts, G.Thomas, D.Blakey, and M.Merrick (2002).
Membrane sequestration of the signal transduction protein GlnK by the ammonium transporter AmtB.
  EMBO J, 21, 536-545.  
11238986 T.Arcondéguy, R.Jack, and M.Merrick (2001).
P(II) signal transduction proteins, pivotal players in microbial nitrogen control.
  Microbiol Mol Biol Rev, 65, 80.  
11277925 Y.Xu, P.D.Carr, T.Huber, S.G.Vasudevan, and D.L.Ollis (2001).
The structure of the PII-ATP complex.
  Eur J Biochem, 268, 2028-2037.  
10754576 A.J.Ninfa, and M.R.Atkinson (2000).
PII signal transduction proteins.
  Trends Microbiol, 8, 172-179.  
10760266 W.C.van Heeswijk, D.Wen, P.Clancy, R.Jaggi, D.L.Ollis, H.V.Westerhoff, and S.G.Vasudevan (2000).
The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade.
  Proc Natl Acad Sci U S A, 97, 3942-3947.  
  10198037 N.Michel-Reydellet, and P.A.Kaminski (1999).
Azorhizobium caulinodans PII and GlnK proteins control nitrogen fixation and ammonia assimilation.
  J Bacteriol, 181, 2655-2658.  
  10430565 P.S.Kessler, and J.A.Leigh (1999).
Genetics of nitrogen regulation in Methanococcus maripaludis.
  Genetics, 152, 1343-1351.  
9811909 M.H.Hsieh, H.M.Lam, F.J.van de Loo, and G.Coruzzi (1998).
A PII-like protein in Arabidopsis: putative role in nitrogen sensing.
  Proc Natl Acad Sci U S A, 95, 13965-13970.  
  9209053 P.Jiang, P.Zucker, M.R.Atkinson, E.S.Kamberov, W.Tirasophon, P.Chandran, B.R.Schefke, and A.J.Ninfa (1997).
Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors.
  J Bacteriol, 179, 4342-4353.  
9312015 R.Jaggi, W.C.van Heeswijk, H.V.Westerhoff, D.L.Ollis, and S.G.Vasudevan (1997).
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.
  EMBO J, 16, 5562-5571.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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