2jgv: Difference between revisions

Revision as of 11:47, 28 July 2008

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File:2jgv.png

Template:STRUCTURE 2jgv

STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADPSTRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP

Template:ABSTRACT PUBMED 17459874

About this StructureAbout this Structure

2JGV is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism., Miallau L, Hunter WN, McSweeney SM, Leonard GA, J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:17459874

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OCA

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-'''STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP'''
+===STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP===
-==Overview==
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-High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified.
+The line below this paragraph, {{ABSTRACT_PUBMED_17459874}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17459874}}
 ==About this Structure==
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 [[Category: Phosphoryl transfer]]
 [[Category: Transferase]]
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