1fjw
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(New page: 200px<br /><applet load="1fjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjw, resolution 1.9Å" /> '''THERMOLYSIN (50 MM PH...)
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Revision as of 12:52, 20 November 2007
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THERMOLYSIN (50 MM PHENOL SOAKED)
Overview
Multiple Solvent Crystal Structures (MSCS) is a crystallographic technique, to identify energetically favorable positions and orientations of small, organic molecules on the surface of proteins. We determined the, high-resolution crystal structures of thermolysin (TLN), generated from, crystals soaked in 50--70% acetone, 50--80% acetonitrile and 50 mM phenol., The structures of the protein in the aqueous-organic mixtures are, essentially the same as the native enzyme and a number of solvent, interaction sites were identified. The distribution of probe molecules, shows clusters in the main specificity pocket of the active site and a, buried subsite. Within the active site, we compared the experimentally, determined solvent positions with predictions from two computational, functional group mapping techniques, GRID and Multiple Copy Simultaneous, Search (MCSS). The experimentally determined small molecule positions are, consistent with the structures of known protein--ligand complexes of TLN.
About this Structure
1FJW is a Single protein structure of sequence from Bacillus thermoproteolyticus with ZN, CA, DMS and IPH as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.
Reference
Experimental and computational mapping of the binding surface of a crystalline protein., English AC, Groom CR, Hubbard RE, Protein Eng. 2001 Jan;14(1):47-59. PMID:11287678
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