1l3f

Thermolysin in the Absence of Substrate has an Open Conformation

spinqualitylabelsall models 1l3f, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1l3f 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: CA, ZN Related: 8tln 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 The bacterial neutral proteases have been proposed to undergo hinge-bending during their catalytic cycle. However, in thermolysin, the prototypical member of the family, no significant conformational change has been observed. The structure of thermolysin has now been determined in a new crystal form that for the first time shows the enzyme in the absence of a ligand bound in the active site. This is shown to be an 'open' form of the enzyme. The relative orientation of the two domains that define the active-site cleft differ by a 5 degrees rotation relative to their positions in the previously studied ligand-bound 'closed' form. Based on structural comparisons, kinetic studies on mutants and molecular-dynamics simulations, Gly78 and Gly135-Gly136 have previously been suggested as two possible hinge regions. Comparison of the 'open' and 'closed' structures suggests that neither of the proposed hinge regions completely accounts for the observed displacement. The concerted movement of a group of side chains suggested to be associated with the hinge-bending motion is, however, confirmed. Thermolysin in the absence of substrate has an open conformation.,Hausrath AC, Matthews BW Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1002-7. Epub, 2002 May 29. PMID:12037302 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thermolysin

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