A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN

Structural analysis of zinc substitutions in the active site of thermolysin.

Structural Comparison Suggests that Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis

Structure of Thermolysin Refined at 1.6 Angstroms Resolution

Structure of a Mercaptan-Thermolysin Complex Illustrates Mode of Inhibition of Zinc Proteases by Substrate-Analogue Mercaptans

Binding of Hydroxamic Acid Inhibitors to Crystalline Thermolysin Suggests a Pentacoordinate Zinc Intermediate in Catalysis

Binding of the Biproduct Analog L-Benzylsuccinic Acid to Thermolysin Determined by X-Ray Crystallography

Comparison of the Structures of Carboxypeptidase a and Thermolysin

A Crystallographic Study of the Complex of Phosphoramidon with Thermolysin. A Model for the Presumed Catalytic Transition State and for the Binding of Extended Substrates

Crystallographic Study of the Binding of Dipeptide Inhibitors to Thermolysin. Implications for the Mechanism of Catalysis

Role of Calcium in the Thermal Stability of Thermolysin

Evidence of Homologous Relationship between Thermolysin and Neutral Protease a of Bacillus Subtilis

Binding of Lanthanide Ions to Thermolysin

The Structure of Thermolysin,an Electron Density Map at 2.3 Angstroms Resolution

Three Dimensional Structure of Thermolysin

National Biomedical Research Foundation, Silver Spring,Md.
Atlas of Protein Sequence and Structure (Data Section)

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT
YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE
SGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKA
AYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK

RESIDUES 1321 AND 1322 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE ACTIVE SITE OF THE MOLECULE. IT IS PRESUMED THAT THE ORIGIN OF THIS DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE PROTEIN. SINCE THE C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES NOT INCORPORATED INTO THE CRYSTAL MUST HAVE BEEN SACRIFICED.

ONE ZINC ION IS THE NATIVE ZINC AND IS BOUND TO HOH 673, HIS 142, HIS 146, AND GLU 166. A SECOND (PARTIALLY-OCCUPIED) ZINC IS BOUND TO HIS 231, TYR 157, GLU 166, AND HOH 673.