PDBsum entry: 1bdg

Hexokinase

PDB id: 1bdg

Contents

Protein chain

444 a.a. *

Ligands

GLC

SO4 ×3

Waters ×104

* Residue conservation analysis

PDB id:

1bdg

Name:

Hexokinase

Title:

Hexokinase from schistosoma mansoni complexed with glucose

Structure:

Hexokinase. Chain: a. Synonym: atp/:d-hexose-6-phosphotransferase. Engineered: yes

Source:

Schistosoma mansoni. Organism_taxid: 6183. Organ: blood. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Monomer (from PDB file)

Resolution:

2.60Å R-factor: 0.173 R-free: 0.256

Authors:

A.M.Mulichak,R.M.Garavito

Key ref:

A.M.Mulichak et al. (1998). The structure of mammalian hexokinase-1. Nat Struct Biol, 5, 555-560. PubMed id: 9665168 DOI: 10.1038/811

Date:

08-May-98 Release date: 11-May-99

Protein chain

Q26609  (HXK_SCHMA) -  Hexokinase

Seq: 451 a.a.

Struc: 444 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.1.1 - Hexokinase.
• Reaction: ATP + D-hexose = ADP + D-hexose 6-phosphate

ATP + D-hexose (Bound ligand (Het Group name = GLC) corresponds exactly) = ADP + D-hexose 6-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: carbohydrate metabolic process (2 terms)
• Biochemical function: nucleotide binding (6 terms)

reference

DOI no: 10.1038/811

Nat Struct Biol 5:555-560 (1998)

PubMed id: 9665168

The structure of mammalian hexokinase-1.

A.M.Mulichak, J.E.Wilson, K.Padmanabhan, R.M.Garavito.

ABSTRACT

We have determined the structures of the glucose-6-phosphate (G6P)-inhibitable 100,000 Mr Type I hexokinase from rat and the G6P-sensitive 50,000 Mr hexokinase from Schistosoma mansoni at a resolution of 2.8 and 2.6 A respectively. The structures define the glucose and G6P binding sites in these enzymes, suggest the mechanisms of intradomain G6P inhibition and activity loss in the Type I hexokinase N-terminal half, and reveal the structure of the membrane targeting motif that integrates the Type I hexokinase into the outer mitochondrial membrane.

Selected figure(s)

Figure 1.
Figure 1. Ribbon drawings of the rHK-I a, dimer and b, monomer. In (b),the strictly helical portion of the linker between the rHK-In and rHK-Ic domains is colored blue with a putative pivot point indicated by an asterisk. The interdomain salt bridges Arg 69−Asp 814 and Asp 251−Arg 801 are indicated with an arrowhead (Asp, red; Arg, blue). In c, a space-filling model shows a domain interface (In), the interdomain salt bridges (Asp, red; Arg, light blue) and the linker (light gray); G6P and glucose denotes their binding sites in the rHK-In and rHK-Ic domains respectively. In all views, the membrane binding peptide is colored gold; Glucose is yellow and G6P is red. Figs 1 and 2b were prepared using Molscript^ 27 and Raster3D^28.

Figure 2.
Figure 2. Views of the crystal contacts along the a-axis in the Type 2 crystals. a, The 2F[o] - F[c] electron density (1 , blue) shows a calcium-mediated salt bridge (*) between Asp 365 from neighboring monomers and one of the well ordered membrane binding peptides (M-I-A-A-Q-L-L-A-Y-Y-F-T-E-L-K-...). F[o] - F[c] electron density (3.5 , orange; 4.5 , red) denotes the calcium site. b, A view of interactions between the antiparallel helical membrane binding peptide dimer.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1998, 5, 555-560) copyright 1998.

Figures were selected by an automated process.