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The crystallographic structure of the subtilisin protease from Penicillium cyclopium.

Published on Jun 1, 1997in Biochemistry2.95
· DOI :10.1021/bi963189t
Stanley Koszelak12
Estimated H-index: 12
,
Joseph D. Ng13
Estimated H-index: 13
+ 3 AuthorsAlexander McPherson53
Estimated H-index: 53
Abstract
The major extracellular protease from the fungus Pencillium cyclopium was crystallized in the presence of p-phenylmethanesulfonyl fluoride (PMSF) and investigated by X-ray diffraction analysis. It was subsequently cloned and the amino acid sequence deduced from its cDNA. Although the sequence is only 49% identical to that of proteinase K of Tritirachium album, the three-dimensional structures of the two proteases are virtually identical. The model for P. cyclopium protease was refined by simulated annealing to an R of 18% at 1.7 A resolution. The greatest variation from the proteinase K polypeptide is in loop 114−134 and is due to the absence of a disulfide bridge in the P. cyclopium protease that is present in proteinase K. A difference was also observed in the orientation of the histidine in the catalytic triad, though this could be due to the presence of PMSF at the active site. The coordination geometry of the strongly bound calcium in the P. cyclopium protease is octahedral and uses some different pr...
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#2T. K. Girish (CSIR-CFTRI: Central Food Technological Research Institute)
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#2Keith J. Chappell (UQ: University of Queensland)H-Index: 11
Last.Jennifer L. Martin (UQ: University of Queensland)H-Index: 46
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#1Katherine E. McAuley (Daresbury Laboratory)H-Index: 15
#2Allan Svendsen (Novozymes)H-Index: 31
Last.Keith S. Wilson (Ebor: University of York)H-Index: 69
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#1R.P. Gupta (DU: University of Delhi)H-Index: 19
#2Qasim Khalil Beg (DU: University of Delhi)H-Index: 22
Last.Bhavna Chauhan (DU: University of Delhi)H-Index: 3
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#1David E. MetzlerH-Index: 30
#2Carol M. MetzlerH-Index: 12
Last.David J. SaukeH-Index: 2
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