8TLN

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

Replaces:  3TLNReplaces:  1TLNReplaces:  2TLN

Summary for 8TLN

• Entry DOI: 10.2210/pdb8tln/pdb
• Descriptor: THERMOLYSIN, VALINE, LYSINE, ... (7 entities in total)
• Functional Keywords: hydrolase(metalloproteinase)
• Biological source: Bacillus thermoproteolyticus
• Cellular location: Secreted: P00800
• Total number of polymer chains: 1
• Total formula weight: 34930.50

Authors

Tronrud, D.,Matthews, B.W. (deposition date: 1993-09-01, release date: 1994-04-30, Last modification date: 2024-02-14)

• Primary citation: Holland, D.R.,Tronrud, D.E.,Pley, H.W.,Flaherty, K.M.,Stark, W.,Jansonius, J.N.,McKay, D.B.,Matthews, B.W.; Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.; Biochemistry, 31:11310-11316, 1992; PubMed: 1445869; DOI: 10.1021/bi00161a008

Experimental method

X-RAY DIFFRACTION (1.6 Å)