2sfa
From Proteopedia
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| - | [[Image:2sfa.jpg|left|200px]] | + | [[Image:2sfa.jpg|left|200px]] |
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| - | '''SERINE PROTEINASE FROM STREPTOMYCES FRADIAE ATCC 14544''' | + | {{Structure |
| + | |PDB= 2sfa |SIZE=350|CAPTION= <scene name='initialview01'>2sfa</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SERINE PROTEINASE FROM STREPTOMYCES FRADIAE ATCC 14544''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SFA is a [ | + | 2SFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_fradiae Streptomyces fradiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SFA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8119298 8119298] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces fradiae]] | [[Category: Streptomyces fradiae]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:17 2008'' |
Revision as of 16:38, 20 March 2008
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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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