1ig8 | pdb_00001ig8

Crystal Structure of Yeast Hexokinase PII with the correct amino acid sequence

spinqualitylabelsall models 1ig8, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ig8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 2yhx Activity: Hexokinase, with EC number 2.7.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HXKB_YEAST] Main glucose phosphorylating enzyme. May play a regulatory role in both induction and repression of gene expression by glucose. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Hexokinase is the first enzyme in the glycolytic pathway, catalyzing the transfer of a phosphoryl group from ATP to glucose to form glucose 6-phosphate and ADP. Two yeast hexokinase isozymes are known, namely PI and PII. The crystal structure of yeast hexokinase PII from Saccharomyces cerevisiae without substrate or competitive inhibitor is determined and refined in a tetragonal crystal form at 2.2-A resolution. The folding of the peptide chain is very similar to that of Schistosoma mansoni and previous yeast hexokinase models despite only 30% sequence identity between them. Distinct differences in conformation are found that account for the absence of glucose in the binding site. Comparison of the current model with S. mansoni and yeast hexokinase PI structures both complexed with glucose shows in atomic detail the rigid body domain closure and specific loop movements as glucose binds. A hydrophobic channel formed by strictly conserved hydrophobic residues in the small domain of the hexokinase is identified. The channel's mouth is close to the active site and passes through the small domain to its surface. The possible role of the observed channel in proton transfer is discussed. The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action.,Kuser PR, Krauchenco S, Antunes OA, Polikarpov I J Biol Chem. 2000 Jul 7;275(27):20814-21. PMID:10749890 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA