1y3g | pdb_00001y3g

Crystal Structure of a Silanediol Protease Inhibitor Bound to Thermolysin

spinqualitylabelsall models 1y3g, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1y3g is a 1 chain structure with sequence from 'bacillus thermoproteolyticus'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3PL, AMM, CA, DMS, LEU, ZN Activity: Thermolysin, with EC number 3.4.24.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [THER_BACTH] Extracellular zinc metalloprotease. 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 Dialkylsilanediols have been found to be an effective functional group for the design of active-site-directed protease inhibitors, including aspartic (HIV protease) and metallo (ACE and thermolysin) proteases. The use of silanediols is predicated on its resemblance to the hydrated carbonyl transition-state structure of amide hydrolysis. This concept has been tested by replacing the presumed tetrahedral carbon of a thermolysin substrate with a silanediol group, resulting in an inhibitor with an inhibition constant K(i) = 40 nM. The structure of the silanediol bound to the active site of thermolysin was found to have a conformation very similar to that of a corresponding phosphonamidate inhibitor (K(i) = 10 nM). In both cases, a single oxygen is within bonding distance to the active-site zinc ion, mimicking the presumed tetrahedral transition state. There are binding differences that appear to be related to the presence or absence of protons on the oxygens attached to the silicon or phosphorus. This is the first crystal structure of an organosilane bound to the active site of a protease. Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin.,Juers DH, Kim J, Matthews BW, Sieburth SM Biochemistry. 2005 Dec 20;44(50):16524-8. PMID:16342943 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thermolysin 3D structures

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