2JG1

STRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE with cofactor and substrate

Summary for 2JG1

• Entry DOI: 10.2210/pdb2jg1/pdb
• Related: 2JGV
• Descriptor: TAGATOSE-6-PHOSPHATE KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: d-tagatose-6-phosphate kinase, phosphoryl transfer, conformational changes, kinase, transferase, lactose metabolism
• Biological source: STAPHYLOCOCCUS AUREUS
• Total number of polymer chains: 4
• Total formula weight: 147707.18

Authors

Miallau, L.,Hunter, W.N.,McSweeney, S.M.,Leonard, G.A. (deposition date: 2007-02-07, release date: 2007-04-24, Last modification date: 2020-07-29)

Primary citation

Miallau, L.,Hunter, W.N.,Mcsweeney, S.M.,Leonard, G.A.
Structures of Staphylococcus Aureus D-Tagatose-6-Phosphate Kinase Implicate Domain Motions in Specificity and Mechanism.
J.Biol.Chem., 282:19948-, 2007

PubMed Abstract: 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.

PubMed: 17459874
DOI: 10.1074/JBC.M701480200

Experimental method

X-RAY DIFFRACTION (2 Å)