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PDBsum entry 1gle

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protein ligands metals Protein-protein interface(s) links
Phosphotransferase PDB id
1gle
Jmol
Contents
Protein chains
161 a.a. *
489 a.a. *
Ligands
G3H
ADP
Metals
_ZN ×2
Waters ×48
* Residue conservation analysis
PDB id:
1gle
Name: Phosphotransferase
Title: Cation promoted association (cpa) of a regulatory and target is controlled by phosphorylation
Structure: Glucose-specific protein iiiglc. Chain: f. Engineered: yes. Glycerol kinase. Chain: g. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Organism_taxid: 562
Biol. unit: Octamer (from PQS)
Resolution:
2.94Å     R-factor:   0.149    
Authors: M.D.Feese,N.D.Meadow,S.Roseman,D.W.Pettigrew,S.J.Remington
Key ref: M.Feese et al. (1994). Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc Natl Acad Sci U S A, 91, 3544-3548. PubMed id: 8170944 DOI: 10.1073/pnas.91.9.3544
Date:
07-Mar-94     Release date:   31-May-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P69783  (PTGA_ECOLI) -  Glucose-specific phosphotransferase enzyme IIA component
Seq:
Struc:
169 a.a.
161 a.a.
Protein chain
Pfam   ArchSchema ?
P0A6F3  (GLPK_ECOLI) -  Glycerol kinase
Seq:
Struc:
502 a.a.
489 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain G: E.C.2.7.1.30  - Glycerol kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + glycerol = ADP + sn-glycerol 3-phosphate
ATP
+ glycerol
=
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly
+
sn-glycerol 3-phosphate
Bound ligand (Het Group name = G3H)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   4 terms 
  Biological process     metabolic process   12 terms 
  Biochemical function     catalytic activity     9 terms  

 

 
    reference    
 
 
DOI no: 10.1073/pnas.91.9.3544 Proc Natl Acad Sci U S A 91:3544-3548 (1994)
PubMed id: 8170944  
 
 
Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation.
M.Feese, D.W.Pettigrew, N.D.Meadow, S.Roseman, S.J.Remington.
 
  ABSTRACT  
 
A central question in molecular biology concerns the means by which a regulatory protein recognizes different targets. IIIGlc, the glucose-specific phosphocarrier protein of the bacterial phosphotransferase system, is also the central regulatory element of the PTS. Binding of unphosphorylated IIIGlc inhibits several non-PTS proteins, but there is little or no sequence similarity between IIIGlc binding sites on different target proteins. The crystal structure of Escherichia coli IIIGlc bound to one of its regulatory targets, glycerol kinase, has been refined at 2.6-A resolution in the presence of products, adenosine diphosphate and glycerol 3-phosphate. Structural and kinetic analyses show that the complex of IIIGlc with glycerol kinase creates an intermolecular Zn(II) binding site with ligation identical to that of the zinc peptidase thermolysin. The zinc is coordinated by the two active-site histidines of IIIGlc, a glutamate of glycerol kinase, and a water molecule. Zn(II) at 0.01 and 0.1 mM decreases the Ki of IIIGlc for glycerol kinase by factors of about 15 and 60, respectively. The phosphorylation of one of the histidines of IIIGlc, in its alternative role as phosphocarrier, provides an elegant means of controlling the cation-enhanced protein-protein regulatory interaction. The need for the target protein to supply only one metal ligand may account for the lack of sequence similarity among the regulatory targets of IIIGlc.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19056335 D.W.Pettigrew (2009).
Amino acid substitutions in the sugar kinase/hsp70/actin superfamily conserved ATPase core of E. coli glycerol kinase modulate allosteric ligand affinity but do not alter allosteric coupling.
  Arch Biochem Biophys, 481, 151-156.  
19819219 D.W.Pettigrew (2009).
Oligomeric interactions provide alternatives to direct steric modes of control of sugar kinase/actin/hsp70 superfamily functions by heterotropic allosteric effectors: inhibition of E. coli glycerol kinase.
  Arch Biochem Biophys, 492, 29-39.  
19201797 J.Diao, and M.S.Hasson (2009).
Crystal structure of butyrate kinase 2 from Thermotoga maritima, a member of the ASKHA superfamily of phosphotransferases.
  J Bacteriol, 191, 2521-2529.
PDB code: 1saz
  17277457 R.Katsumi, Y.Koga, D.J.You, H.Matsumura, K.Takano, and S.Kanaya (2007).
Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 126-129.  
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.  
12829462 P.Grayson, E.Tajkhorshid, and K.Schulten (2003).
Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics.
  Biophys J, 85, 36-48.  
12161559 A.C.Pawlyk, and D.W.Pettigrew (2002).
Transplanting allosteric control of enzyme activity by protein-protein interactions: coupling a regulatory site to the conserved catalytic core.
  Proc Natl Acad Sci U S A, 99, 11115-11120.  
11418773 H.S.Huang, T.Inoue, K.Ito, and T.Yoshimoto (2001).
Preliminary crystallographic study of Thermus aquaticus glycerol kinase.
  Acta Crystallogr D Biol Crystallogr, 57, 1030-1031.  
11106599 A.Gorokhov, L.Perera, T.A.Darden, M.Negishi, L.C.Pedersen, and L.G.Pedersen (2000).
Heparan sulfate biosynthesis: a theoretical study of the initial sulfation step by N-deacetylase/N-sulfotransferase.
  Biophys J, 79, 2909-2917.  
10651627 S.G.Hymowitz, M.P.O'Connell, M.H.Ultsch, A.Hurst, K.Totpal, A.Ashkenazi, A.M.de Vos, and R.F.Kelley (2000).
A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL.
  Biochemistry, 39, 633-640.
PDB code: 1dg6
10393270 G.T.Robillard, and J.Broos (1999).
Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system.
  Biochim Biophys Acta, 1422, 73.  
  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.  
9538005 D.W.Pettigrew, N.D.Meadow, S.Roseman, and S.J.Remington (1998).
Cation-promoted association of Escherichia coli phosphocarrier protein IIAGlc with regulatory target protein glycerol kinase: substitutions of a Zinc(II) ligand and implications for inducer exclusion.
  Biochemistry, 37, 4875-4883.  
9817843 M.D.Feese, H.R.Faber, C.E.Bystrom, D.W.Pettigrew, and S.J.Remington (1998).
Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
  Structure, 6, 1407-1418.
PDB codes: 1bu6 1glf
9054511 M.Kato, T.Mizuno, T.Shimizu, and T.Hakoshima (1997).
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB.
  Cell, 88, 717-723.
PDB code: 1a0b
9434897 M.M.McEvoy, and F.W.Dahlquist (1997).
Phosphohistidines in bacterial signaling.
  Curr Opin Struct Biol, 7, 793-797.  
9188690 P.P.Zhu, N.Nosworthy, A.Ginsburg, M.Miyata, Y.J.Seok, and A.Peterkofsky (1997).
Expression, purification, and characterization of enzyme IIA(glc) of the phosphoenolpyruvate:sugar phosphotransferase system of Mycoplasma capricolum.
  Biochemistry, 36, 6947-6953.  
8628731 D.L.Gerloff, and F.E.Cohen (1996).
Secondary structure prediction and unrefined tertiary structure prediction for cyclin A, B, and D.
  Proteins, 24, 18-34.  
  8631672 D.W.Pettigrew, W.Z.Liu, C.Holmes, N.D.Meadow, and S.Roseman (1996).
A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo.
  J Bacteriol, 178, 2846-2852.  
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.