3hr7 | pdb_00003hr7

Crystal structure of the shikimate kinase-sulfate complex from Helicobacter pylori

spinqualitylabelsall models 3hr7, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hr7 is a 2 chain structure with sequence from Campylobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 1zuh, 1zui Gene: aroK (Campylobacter pylori) Activity: Shikimate kinase, with EC number 2.7.1.71 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AROK_HELPY] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Shikimate kinase (SK), which catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP, is the enzyme in the fifth step of the shikimate pathway for biosynthesis of aromatic amino acids. This pathway is present in bacteria, fungi, and plants but absent in mammals and therefore represents an attractive target pathway for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here we investigated the detailed structure-activity relationship of SK from Helicobacter pylori (HpSK). Site-directed mutagenesis and isothermal titration calorimetry studies revealed critical conserved residues (D33, F48, R57, R116, and R132) that interact with shikimate and are therefore involved in catalysis. Crystal structures of HpSK.SO(4), R57A, and HpSK*shikimate-3-phosphate * ADP show a characteristic three-layer architecture and a conformationally elastic region consisting of F48, R57, R116, and R132, occupied by shikimate. The structure of the inhibitor complex, E114A * 162535, was also determined, which revealed a dramatic shift in the elastic LID region and resulted in conformational locking into a distinctive form. These results reveal considerable insight into the active-site chemistry of SKs and a selective inhibitor-induced-fit mechanism. Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism.,Cheng WC, Chen YF, Wang HJ, Hsu KC, Lin SC, Chen TJ, Yang JM, Wang WC PLoS One. 2012;7(3):e33481. Epub 2012 Mar 16. PMID:22438938 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Shikimate kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA