Structural highlights
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 mode of binding to thermolysin of the ester analog Cbz-GlyP-(O)-Leu-Leu has been determined by x-ray crystallography and shown to be virtually identical (maximum difference 0.2 angstrom) with the corresponding peptide analog Cbz-GlyP-(NH)-Leu-Leu. The two inhibitors provide a matched pair of enzyme-inhibitor complexes that differ by 4.1 kilocalories per mole in intrinsic binding energy but are essentially identical except for the presence or absence of a specific hydrogen bond.
Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.,Tronrud DE, Holden HM, Matthews BW Science. 1987 Jan 30;235(4788):571-4. PMID:3810156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tronrud DE, Holden HM, Matthews BW. Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond. Science. 1987 Jan 30;235(4788):571-4. PMID:3810156
