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PDBsum entry 1gpr

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protein links
Phosphotransferase PDB id
1gpr
Jmol
Contents
Protein chain
158 a.a. *
Waters ×100
* Residue conservation analysis
PDB id:
1gpr
Name: Phosphotransferase
Title: Refined crystal structure of iia domain of the glucose permease of bacillus subtilis at 1.9 angstroms resolution
Structure: Glucose permease. Chain: a. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423
Biol. unit: Dimer (from PQS)
Resolution:
1.90Å     R-factor:   0.156    
Authors: D.-I.Liao,O.Herzberg
Key ref:
D.I.Liao et al. (1991). Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution. Biochemistry, 30, 9583-9594. PubMed id: 1911744 DOI: 10.1021/bi00104a004
Date:
25-Sep-91     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q59250  (Q59250_BACIU) -  Protein-N(Pi)-phosphohistidine-sugar phosphotransferase
Seq:
Struc:
162 a.a.
158 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.69  - Protein-N(pi)-phosphohistidine--sugar phosphotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate

+
=
+
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     transport   6 terms 
  Biochemical function     transferase activity     4 terms  

 

 
    Key reference    
 
 
DOI no: 10.1021/bi00104a004 Biochemistry 30:9583-9594 (1991)
PubMed id: 1911744  
 
 
Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution.
D.I.Liao, G.Kapadia, P.Reddy, M.H.Saier, J.Reizer, O.Herzberg.
 
  ABSTRACT  
 
The crystal structure of the IIA domain of the glucose permease of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.2-A resolution. Refinement of the structure is in progress, and the current R-factor is 0.201 (R = sigma h parallel Fo magnitude of - Fc parallel/sigma h magnitude of Fo, where magnitude of Fo and magnitude of Fc are the observed and calculated structure factor amplitudes, respectively) for data between 6.0- and 2.2-A resolution for which F greater than or equal to 2 sigma (F). This is an antiparallel beta-barrel structure that incorporates "Greek key" and "jellyroll" topological motifs. A shallow depression is formed at the active site by part of the beta-sheet and an omega-loop flanking one side of the sheet. His83, the histidyl residue which is the phosphorylation target of HPr and which transfers the phosphoryl group to the IIB domain of the permease, is located at the C-terminus of a beta-strand. The N epsilon atom is partially solvated and also interacts with the N epsilon atom of a second histidyl residue, His68, located at the N-terminus of an adjacent beta-strand, suggesting they share a proton. The geometry of the hydrogen bond is imperfect, though. Electrostatic interactions with other polar groups and van der Waals contacts with the side chains of two flanking phenylalanine residues assure the precise orientation of the imidazole rings. The hydrophobic nature of the surface around the His83-His68 pair may be required for protein-protein recognition by HPr or/and by the IIB domain of the permease. The side chains of two aspartyl residues, Asp31 and Asp87, are oriented toward each other across a narrow groove, about 7 A from the active-site His83, suggesting they may play a role in protein-protein interaction. A model of the phosphorylated form of the molecule is proposed, in which oxygen atoms of the phosphoryl group interact with the side chain of His68 and with the main-chain nitrogen atom of a neighboring residue, Val89. The model, in conjunction with previously reported site-directed mutagenesis experiments, suggests that the phosphorylation of His83 may be accompanied by the protonation of His68. This may be important for the interaction with the IIB domain of the permease and/or play a catalytic role in the phosphoryl transfer from IIA to IIB.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17158705 J.Deutscher, C.Francke, and P.W.Postma (2006).
How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
  Microbiol Mol Biol Rev, 70, 939.  
16443929 J.Y.Suh, M.Cai, D.C.Williams, and G.M.Clore (2006).
Solution structure of a post-transition state analog of the phosphotransfer reaction between the A and B cytoplasmic domains of the mannitol transporter IIMannitol of the Escherichia coli phosphotransferase system.
  J Biol Chem, 281, 8939-8949.
PDB code: 2few
16407305 O.Khersonsky, and D.S.Tawfik (2006).
The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases.
  J Biol Chem, 281, 7649-7656.  
15741344 G.Wang, A.Peterkofsky, P.A.Keifer, and X.Li (2005).
NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
  Protein Sci, 14, 1082-1090.  
15185334 A.D.Mackerell, M.Feig, and C.L.Brooks (2004).
Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations.
  J Comput Chem, 25, 1400-1415.  
12116391 D.J.Price, and C.L.Brooks (2002).
Modern protein force fields behave comparably in molecular dynamics simulations.
  J Comput Chem, 23, 1045-1057.  
12202490 G.Cornilescu, B.R.Lee, C.C.Cornilescu, G.Wang, A.Peterkofsky, and G.M.Clore (2002).
Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system.
  J Biol Chem, 277, 42289-42298.
PDB code: 1j6t
11060015 G.Wang, J.M.Louis, M.Sondej, Y.J.Seok, A.Peterkofsky, and G.M.Clore (2000).
Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.
  EMBO J, 19, 5635-5649.
PDB code: 1ggr
  9882680 M.G.Gunnewijk, P.W.Postma, and B.Poolman (1999).
Phosphorylation and functional properties of the IIA domain of the lactose transport protein of Streptococcus thermophilus.
  J Bacteriol, 181, 632-641.  
  9457881 P.Reddy, and M.Kamireddi (1998).
Modulation of Escherichia coli adenylyl cyclase activity by catalytic-site mutants of protein IIA(Glc) of the phosphoenolpyruvate:sugar phosphotransferase system.
  J Bacteriol, 180, 732-736.  
9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
  Annu Rev Biophys Biomol Struct, 26, 597-627.  
9109646 D.S.Garrett, Y.J.Seok, A.Peterkofsky, G.M.Clore, and A.M.Gronenborn (1997).
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
  Biochemistry, 36, 4393-4398.  
9054557 D.S.Garrett, Y.J.Seok, D.I.Liao, A.Peterkofsky, A.M.Gronenborn, and G.M.Clore (1997).
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
  Biochemistry, 36, 2517-2530.
PDB codes: 1eza 1ezb 1ezc 1ezd
9200688 G.Gemmecker, M.Eberstadt, A.Buhr, R.Lanz, S.G.Grdadolnik, H.Kessler, and B.Erni (1997).
Glucose transporter of Escherichia coli: NMR characterization of the phosphocysteine form of the IIB(Glc) domain and its binding interface with the IIA(Glc) subunit.
  Biochemistry, 36, 7408-7417.  
9030753 S.Seip, R.Lanz, R.Gutknecht, K.Flükiger, and B.Erni (1997).
The fructose transporter of Bacillus subtilis encoded by the lev operon: backbone assignment and secondary structure of the IIB(Lev) subunit.
  Eur J Biochem, 243, 306-314.  
8774730 F.Huber, and B.Erni (1996).
Membrane topology of the mannose transporter of Escherichia coli K12.
  Eur J Biochem, 239, 810-817.  
8784182 M.Eberstadt, S.G.Grdadolnik, G.Gemmecker, H.Kessler, A.Buhr, and B.Erni (1996).
Solution structure of the IIB domain of the glucose transporter of Escherichia coli.
  Biochemistry, 35, 11286-11292.
PDB code: 1iba
8662917 S.Mukhija, and B.Erni (1996).
Purification by Ni2+ affinity chromatography, and functional reconstitution of the transporter for N-acetylglucosamine of Escherichia coli.
  J Biol Chem, 271, 14819-14824.  
8611583 W.Meijberg, G.K.Schuurman-Wolters, and G.T.Robillard (1996).
Interdomain interactions between the hydrophilic domains of the mannitol transporter of Escherichia coli in the unphosphorylated and phosphorylated states.
  Biochemistry, 35, 2759-2766.  
7815935 M.H.Saier, and J.Reizer (1994).
The bacterial phosphotransferase system: new frontiers 30 years later.
  Mol Microbiol, 13, 755-764.  
  7703858 P.P.Zhu, J.Reizer, and A.Peterkofsky (1994).
Unique dicistronic operon (ptsI-crr) in Mycoplasma capricolum encoding enzyme I and the glucose-specific enzyme IIA of the phosphoenolpyruvate:sugar phosphotransferase system: cloning, sequencing, promoter analysis, and protein characterization.
  Protein Sci, 3, 2115-2128.  
  8401218 G.J.Kroon, J.Grötzinger, K.Dijkstra, R.M.Scheek, and G.T.Robillard (1993).
Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy.
  Protein Sci, 2, 1331-1341.  
  7686067 J.Reizer, C.Hoischen, A.Reizer, T.N.Pham, and M.H.Saier (1993).
Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.
  Protein Sci, 2, 506-521.  
8432744 M.H.Saier (1993).
Regulatory interactions involving the proteins of the phosphotransferase system in enteric bacteria.
  J Cell Biochem, 51, 62-68.  
  8246840 P.W.Postma, J.W.Lengeler, and G.R.Jacobson (1993).
Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.
  Microbiol Rev, 57, 543-594.  
8398213 W.Hengstenberg, D.Kohlbrecher, E.Witt, R.Kruse, I.Christiansen, D.Peters, R.Pogge von Strandmann, P.Städtler, B.Koch, and H.R.Kalbitzer (1993).
Structure and function of proteins of the phosphotransferase system and of 6-phospho-beta-glycosidases in gram-positive bacteria.
  FEMS Microbiol Rev, 12, 149-163.  
8432747 Y.Chen, W.J.Fairbrother, and P.E.Wright (1993).
Three-dimensional structures of the central regulatory proteins of the bacterial phosphotransferase system, HPr and enzyme IIAglc.
  J Cell Biochem, 51, 75-82.  
  1304914 J.Reizer, A.Reizer, M.H.Saier, and G.R.Jacobson (1992).
A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria.
  Protein Sci, 1, 722-726.  
1549615 O.Herzberg, P.Reddy, S.Sutrina, M.H.Saier, J.Reizer, and G.Kapadia (1992).
Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.
  Proc Natl Acad Sci U S A, 89, 2499-2503.  
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 code is shown on the right.