1s4e: Difference between revisions

Revision as of 03:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s4e.png

Template:STRUCTURE 1s4e

Pyrococcus furiosus galactokinase in complex with galactose, ADP and magnesiumPyrococcus furiosus galactokinase in complex with galactose, ADP and magnesium

Template:ABSTRACT PUBMED 15003454

About this StructureAbout this Structure

1S4E is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

Substrate specificity and mechanism from the structure of Pyrococcus furiosus galactokinase., Hartley A, Glynn SE, Barynin V, Baker PJ, Sedelnikova SE, Verhees C, de Geus D, van der Oost J, Timson DJ, Reece RJ, Rice DW, J Mol Biol. 2004 Mar 19;337(2):387-98. PMID:15003454

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Pyrococcus furiosus galactokinase in complex with galactose, ADP and magnesium'''
+===Pyrococcus furiosus galactokinase in complex with galactose, ADP and magnesium===
-==Overview==
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-Galactokinase (GalK) catalyses the first step of the Leloir pathway of galactose metabolism, the ATP-dependent phosphorylation of galactose to galactose-1-phosphate. In man, defects in galactose metabolism can result in disorders with severe clinical consequences, and deficiencies in galactokinase have been linked with the development of cataracts within the first few months of life. The crystal structure of GalK from Pyrococcus furiosus in complex with MgADP and galactose has been determined to 2.9 A resolution to provide insights into the substrate specificity and catalytic mechanism of the enzyme. The structure consists of two domains with the active site in a cleft at the domain interface. Inspection of the substrate binding pocket identifies the amino acid residues involved in galactose and nucleotide binding and points to both structural and mechanistic similarities with other enzymes of the GHMP kinase superfamily to which GalK belongs. Comparison of the sequence of the Gal3p inducer protein, which is related to GalK and which forms part of the transcriptional activation of the GAL gene cluster in the yeast Saccharomyces cerevisiae, has led to an understanding of the molecular basis of galactose and nucleotide recognition. Finally, the structure has enabled us to further our understanding on the functional consequences of mutations in human GalK which cause galactosemia.
+The line below this paragraph, {{ABSTRACT_PUBMED_15003454}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Ghmp kinase superfamily]]
 [[Category: P-loop]]
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