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==Overview== | ==Overview== | ||
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, ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
2JGV is a | 2JGV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tagatose-6-phosphate_kinase Tagatose-6-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.144 2.7.1.144] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JGV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 15:48, 5 November 2007
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STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE IN COMPLEX WITH ADP
OverviewOverview
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.
About this StructureAbout this Structure
2JGV is a Single protein structure of sequence from Staphylococcus aureus with ADP as ligand. Active as Tagatose-6-phosphate kinase, with EC number 2.7.1.144 Structure known Active Site: AC1. 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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