Structure of thermolysin refined at 1.6 Å resolution

摘要: Abstract The structure of the thermostable protease thermolysin has been refined by a restrained least-squares procedure at nominal resolution 1.6 A to conventional R-value 21.3% for 34,671 observed reflections (or R = 19.5% with F0 > 3σ(F0)). was constrained adhere known stereochemistry, root-mean-square deviations 0.021 from ideal bond lengths and 2.9 ° angles. final model included 173 solvent molecules, which were given unit occupancies. Seven these are “buried” within protein. Atoms least apparent thermal motion tend be those that most deeply buried two domains structure. active-site zinc is shown have approximately tetrahedral co-ordination. Unusual features structure, confirmed refinement, include cis-proline, γ-turn, single turn left-handed α-helix. refinement shows does not contain unusual structures supports our previous assertion thermostability proteins in general due combination factors which, different instances, can hydrophobic interactions, hydrogen bonding, ionic disulfide linkages, metal binding other forms stabilization.