1l3f
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(New page: 200px<br /><applet load="1l3f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3f, resolution 2.3Å" /> '''Thermolysin in the Ab...)
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Revision as of 18:05, 20 November 2007
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Thermolysin in the Absence of Substrate has an Open Conformation
Overview
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.
About this Structure
1L3F is a Single protein structure of sequence from Bacillus thermoproteolyticus with CA and ZN as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.
Reference
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
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