2sfa
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(New page: 200px<br /><applet load="2sfa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sfa, resolution 1.6Å" /> '''SERINE PROTEINASE FRO...)
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Revision as of 11:53, 21 November 2007
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SERINE PROTEINASE FROM STREPTOMYCES FRADIAE ATCC 14544
Overview
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.
About this Structure
2SFA is a Single protein structure of sequence from Streptomyces fradiae. Full crystallographic information is available from OCA.
Reference
Purification, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544., Kitadokoro K, Tsuzuki H, Nakamura E, Sato T, Teraoka H, Eur J Biochem. 1994 Feb 15;220(1):55-61. PMID:8119298
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