1MEE

THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C

Summary for 1MEE

• Entry DOI: 10.2210/pdb1mee/pdb
• Descriptor: MESENTERICOPEPTIDASE, EGLIN C, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: complex(serine proteinase-inhibitor)
• Biological source: Bacillus pumilus; More
• Cellular location: Secreted: P07518
• Total number of polymer chains: 2
• Total formula weight: 35202.08

Authors

Dauter, Z.,Betzel, C.,Wilson, K.S. (deposition date: 1991-04-15, release date: 1992-10-15, Last modification date: 2024-02-14)

Primary citation

Dauter, Z.,Betzel, C.,Genov, N.,Pipon, N.,Wilson, K.S.
Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
Acta Crystallogr.,Sect.B, 47:707-730, 1991

PubMed Abstract: The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.

PubMed: 1793542
DOI: 10.1107/S0108768191004202

Experimental method

X-RAY DIFFRACTION (2 Å)