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GlucokinaseGlucokinase

The enzyme glucokinase facilitates phosphorylation of glucose to glucose-6-phosphate. In humans and most other vertebrates glucokinase is used in the liver, the pancreas, the gut and brain. It plays an important role in regulating carbohydrate metabolism, triggering shifts in the cell in response to glucose level: glucokinase is a sort of a glucose sensor. It only phosphorylates glucose if its concetnration is high enough. The structure of glucokinase reveals an allosteric site through which small molecules may modulate the kinetic properties of the enzyme; a property that is the basis for the enzyme use in type 2 diabetes treatment.

Structure

1v4s, resolution 2.30Å ()

Ligands:

, ,

Activity:

Hexokinase, with EC number 2.7.1.1

Related:

1v4t

Structural annotation:
Resources:	InterPro : Ipr001312 Pfam : PF00349, PF03727 SCOP : d1v4sa2, d1v4sa1 UniProt : P35557

Functional annotation:
Biological process:	glucose homeostasis detection of glucose positive regulation of glycogen biosynthetic process glucose metabolic process glycolysis negative regulation of gluconeogenesis positive regulation of insulin secretion
Molecular function:	glucokinase activity kinase activity nucleotide binding hexokinase activity transferase activity ATP binding protein binding glucose binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

The glucokinase has 18 (unless we counted wrong), 13 (this one is for sure), and 3 : a , amide or MRK in short, and last a sugar (alpha-d-glucose) or simply GLC.

Purple denotes all the sections of the protein: the hydrophillic areas that dominate the outer surface which comes in contact with aqueous environments. In this view we can see very neatly how the beta sheets alternate in polarity in a 'zigzag manner, and how the alpha helices are roughly 2-3 polar (while the inner protein is obviously hydrophobic). The , in particular, shows how the surface is dominantly hydrophillic.

ReferenceReference

http://www.proteopedia.org/wiki/index.php/1v4s http://en.wikipedia.org/wiki/Glucokinase

--Tinuke (Abike etc. etc. etc.) Adeyemi and Niva Ran

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