2SFA

SERINE PROTEINASE FROM STREPTOMYCES FRADIAE ATCC 14544

Summary for 2SFA

• Entry DOI: 10.2210/pdb2sfa/pdb
• Descriptor: SERINE PROTEINASE (2 entities in total)
• Functional Keywords: hydrolase, serine protease
• Biological source: Streptomyces fradiae
• Cellular location: Secreted: P41140
• Total number of polymer chains: 1
• Total formula weight: 19014.66

Authors

Kitadokoro, K.,Tsuzuki, H. (deposition date: 1994-04-25, release date: 1996-06-20, Last modification date: 2024-11-20)

Primary citation

Kitadokoro, K.,Tsuzuki, H.,Nakamura, E.,Sato, T.,Teraoka, H.
Purification, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544.
Eur.J.Biochem., 220:55-61, 1994

PubMed Abstract: A proteinase having wide substrate specificity was isolated from Streptomyces fradiae ATCC 14544. This proteinase, which we propose to call SFase-2, was purified from the culture filtrate by S-Sepharose chromatography. The purified enzyme showed an apparent molecular mass of 19 kDa on SDS/PAGE. When synthetic peptides were used as substrates, SFase-2 showed broad substrate specificity. It also hydrolyzed keratin, elastin and collagen as proteinaceous substrates. It was completely inhibited by diisopropylfluorophosphate and chymostatin, but not by tosylphenylalaninechloromethane, tosyllysinechloromethane or EDTA, indicating that it can be classified as a serine proteinase. The matured protein sequence of SFase-2 was determined by a combination of amino acid sequencing and the DNA sequencing of the gene. SFase-2, consisting of 191 amino acids, is a novel proteinase. It showed 76% similarity in the amino acid sequence with Streptomyces griseus proteinase A [Johnson P. and Smillie L. B. (1974) FEBS Lett. 47, 1-6]. For insight into the three-dimensional structure of SFase-2, we obtained single crystals by the vapor diffusion method using sodium phosphate as a precipitant. These crystals belonged to the orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 6.92 nm, b = 7.28 nm, c = 2.99 nm; one molecule was present in the asymmetric unit.

PubMed: 8119298
DOI: 10.1111/j.1432-1033.1994.tb18598.x

Experimental method

X-RAY DIFFRACTION (1.6 Å)