1y34 | pdb_00001y34

Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 E60A mutant

spinqualitylabelsall models 1y34, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1y34 is a 2 chain structure with sequence from Bacillus amyloliquefaciens and Hordeum vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: 15P, CA, CIT, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SUBT_BACAM Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin. 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 A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues involved in intramolecular interactions that shape and constrain the binding loop, were studied to determine their relative importance for inhibition of the serine protease subtilisin BPN', and for resistance of the inhibitor to proteolysis. These functional properties were investigated in tandem with the crystal structures of the mutant inhibitor-enzyme complexes. A dense hydrogen bonding network that supports the binding loop in the vicinity of the scissile bond was found to be important both for enzyme affinity and for stability to proteolysis. Structural analysis, in combination with biochemical measurements, allows differentiation of the structural components most important for resistance to proteolysis and/or binding. The most critical participating residues in the network were found to be Thr-58, Glu-60, Arg-65, and Gly-83. Glu-60 is more important for resistance to proteolysis than for binding, while Arg-65 and two other Arg residues play a greater role in binding than in resistance to proteolysis. Structural comparisons reveal a wide variety of subtle conformational changes in response to mutation, with built-in robustness in the hydrogen bond network, such that loss of one contact is compensated by other new contacts. Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2.,Radisky ES, Lu CJ, Kwan G, Koshland DE Jr Biochemistry. 2005 May 10;44(18):6823-30. PMID:15865427 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin inhibitor 3D structures Subtilisin 3D structures

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