Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2 A resolution.
The crystal structure of thermitase from Thermoactinomyces vulgaris has been determined by x-ray diffraction at 2.2 A resolution. The structure was solved by a combination of single isomorphous replacement and molecular replacement methods. The structure was refined to a conventional R factor of 0.24 using restrained least square procedures CORELS and PROLSQ. The tertiary structure of thermitase is similar to that of subtilsin BPN'. The greatest differences between these structures are related to the insertions and deletions in the sequence.
Teplyakov
A V
AV
Institute of Crystallography, Acad. Sci., USSR.
Kuranova
I P
IP
Harutyunyan
E H
EH
Frömmel
C
C
Höhne
W E
WE
D000192:Actinomycetales / Q000201:enzymology*; D000595:Amino Acid Sequence; D003460:Crystallization; D010450:Endopeptidases; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases; D013381:Subtilisins; D014961:X-Ray Diffraction
D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins; C022728:thermitase