2dfn
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Structure of shikimate kinase from Mycobacterium tuberculosis complexed with ADP and shikimate at 1.9 angstrons of resolution
OverviewOverview
Bacteria, fungi and plants can convert carbohydrate and, phosphoenolpyruvate into chorismate, which is the precursor of various, aromatic compounds. The seven enzymes of the shikimate pathway are, responsible for this conversion. Shikimate kinase (SK) is the fifth enzyme, in this pathway and converts shikimate to shikimate-3-phosphate. In this, work, the conformational changes that occur on binding of shikimate, magnesium and chloride ions to SK from Mycobacterium tuberculosis (MtSK), are described. It was observed that both ions and shikimate influence the, conformation of residues of the active site of MtSK. Magnesium influences, the conformation of the shikimate hydroxyl groups and the position of the, side chains of some of the residues of the active site. Chloride seems to, influence the affinity of ADP and its position in the active site and the, opening length of the LID domain. Shikimate binding causes a closing of, the LID domain and also seems to influence the crystallographic packing of, SK. The results shown here could be useful for understanding the catalytic, mechanism of SK and the role of ions in the activity of this protein.
About this StructureAbout this Structure
2DFN is a Single protein structure of sequence from Mycobacterium tuberculosis with CL, ADP and SKM as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Full crystallographic information is available from OCA.
ReferenceReference
Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis., Dias MV, Faim LM, Vasconcelos IB, de Oliveira JS, Basso LA, Santos DS, de Azevedo WF Jr, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):1-6. Epub 2006 Dec 16. PMID:17183161
Page seeded by OCA on Wed Nov 21 09:35:23 2007