Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 A resolution

Journal of Molecular Biology
J YangJ W Quail

Abstract

The crystal structure of the aspartic proteinase from Rhizomucor miehei (RMP, EC 3. 4. 23. 23) has been refined to 2.15 A resolution to a crystallographic R-value of 0.215 and an Rfree of 0.281. The root-mean-square (r.m.s.) error for the atomic coordinates estimated from a Luzzati plot is 0.2 A. The r.m.s. deviations for the bond distances and bond angles from ideality are 0.01 A and 1.7 degrees, respectively. RMP contains two domains that consist predominantly of beta-sheets. A large substrate-binding cleft is clearly visible between the two domains, and the two catalytic residues Asp38 and Asp237 are located in the middle of the cleft with a water molecule bridging the carboxyl groups of Asp38 and Asp237. Due to crystal packing, the C-terminal domain is more mobile than the N-terminal domain. Most of the aspartic proteinases (except renin) reach their maximum activity at acidic pH. We propose that the optimum pH of each aspartic proteinase is determined by the electrostatic potential at the active site, which, in turn, is determined by the positions and orientations of all the residues near the active site. RMP is the most glycosylated among the aspartic proteinases. The carbohydrate moieties are linked to Asn79 and Asn188. ...Continue Reading

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Citations

Mar 23, 2012·Animal : an International Journal of Animal Bioscience·A FerrariJ Leoni
Sep 7, 2000·Microbiology and Molecular Biology Reviews : MMBR·R MaheshwariM K Bhat
Mar 30, 2010·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Lara GiussaniSalvatore Coluccia
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Sep 6, 2011·Journal of Agricultural and Food Chemistry·Hassan Abd El-BakyRalf Günter Berger
Mar 1, 2009·Marine Genomics·Viviana De LucaClemente Capasso

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