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Transferase PDB id
1hkg
Jmol
Contents
Protein chain
457 a.a.
PDB id:
1hkg
Name: Transferase
Title: Structural dynamics of yeast hexokinase during catalysis
Structure: Hexokinase a. Chain: a. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
Resolution:
3.50Å     R-factor:   not given    
Authors: W.S.Bennettjunior,T.A.Steitz
Key ref: T.A.Steitz et al. (1981). Structural dynamics of yeast hexokinase during catalysis. Philos Trans R Soc Lond B Biol Sci, 293, 43-52. PubMed id: 6115422
Date:
22-Dec-80     Release date:   26-Feb-81    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04806  (HXKA_YEAST) -  Hexokinase-1
Seq:
Struc: 		485 a.a.
457 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 316 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.1  - Hexokinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + D-hexose = ADP + D-hexose 6-phosphate
ATP
 + D-hexose
 = ADP
 + D-hexose 6-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     phosphotransferase activity, alcohol group as acceptor     2 terms  

 

 
    reference    
 
 
Philos Trans R Soc Lond B Biol Sci 293:43-52 (1981)
PubMed id: 6115422  
 
 
Structural dynamics of yeast hexokinase during catalysis.
T.A.Steitz, M.Shoham, W.S.Bennett.
 
  ABSTRACT  
 
The binding of the substrate glucose to yeast hexokinase results in a substantial enzyme conformational change that is essential for catalysis and may be important for the enzyme's specificity, as well as the control of its activity. From high-resolution crystal structures of the monomeric enzyme crystallized both in the presence and in the absence of glucose, we find that glucose binds into the deep cleft that separates the molecule into two lobes and causes these two lobes to move together and close off the cleft. The structure of the hexokinase crystallized in the presence of xylose and ADP is being determined at low resolution. In this crystal form, the enzyme was thought to be in the conformation of the ternary complex. However, a low-resolution structure of this crystal form shows clearly that the enzyme is in the 'open' form and is not a ternary complex. Crystals of the A isozyme with glucose and ADP may be. Further, chemically sequenced tryptic peptides are being incorporated into the model obtained by crystallographic refinement at 2.1 A resolution. Completion of the sequence and the structure of the ternary complex should allow a detailed description of the enzymatic mechanism of this kinase and the role of substrate-induced conformational changes in catalysis and control.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20421461 S.S.Taylor, and A.P.Kornev (2010).
Yet another "active" pseudokinase, Erb3.
  Proc Natl Acad Sci U S A, 107, 8047-8048.  
18647240 N.D.Thomsen, and J.M.Berger (2008).
Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.
  Mol Microbiol, 69, 1071-1090.  
  17565189 E.B.Kuettner, T.M.Kriegel, A.Keim, M.Naumann, and N.Sträter (2007).
Crystallization and preliminary X-ray diffraction studies of hexokinase KlHxk1 from Kluyveromyces lactis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 430-433.  
15466045 V.V.Lunin, Y.Li, J.D.Schrag, P.Iannuzzi, M.Cygler, and A.Matte (2004).
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.
  J Bacteriol, 186, 6915-6927.
PDB codes: 1q18 1sz2
11960978 R.D.Miles, A.Gorrell, and J.G.Ferry (2002).
Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila.
  J Biol Chem, 277, 22547-22552.  
9874766 L.D.Belmont, A.Orlova, D.G.Drubin, and E.H.Egelman (1999).
A change in actin conformation associated with filament instability after Pi release.
  Proc Natl Acad Sci U S A, 96, 29-34.  
1323828 P.Bork, C.Sander, and A.Valencia (1992).
An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.
  Proc Natl Acad Sci U S A, 89, 7290-7294.  
  3519210 H.Muirhead, D.A.Clayden, D.Barford, C.G.Lorimer, L.A.Fothergill-Gilmore, E.Schiltz, and W.Schmitt (1986).
The structure of cat muscle pyruvate kinase.
  EMBO J, 5, 475-481.  
6743743 B.Bunow, and S.R.Caplan (1984).
Determination of the distribution of catalyst activity across a permeable membrane containing an immobilized enzyme. Indeterminacy of a functional approach to a structural problem.
  Biophys J, 45, 1065-1071.  
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.