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Structure paper

TitleStructural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.
Journal, issue, pagesBiochemistry, Vol. 31, Page 11310-11316, Year 1992
Publish dateSep 1, 1993 (structure data deposition date)
AuthorsHolland, D.R. / Tronrud, D.E. / Pley, H.W. / Flaherty, K.M. / Stark, W. / Jansonius, J.N. / McKay, D.B. / Matthews, B.W.
External linksBiochemistry / PubMed:1445869
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-8tln:
STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-VAL:
VALINE

ChemComp-LYS:
LYSINE

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-HOH:
WATER

Source
  • bacillus thermoproteolyticus (bacteria)
KeywordsHYDROLASE(METALLOPROTEINASE)

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