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1arb
From Proteopedia
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| - | [[Image:1arb.jpg|left|200px]] | + | [[Image:1arb.jpg|left|200px]] |
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| - | '''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE''' | + | {{Structure |
| + | |PDB= 1arb |SIZE=350|CAPTION= <scene name='initialview01'>1arb</scene>, resolution 1.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysyl_endopeptidase Lysyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.50 3.4.21.50] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ARB is a [ | + | 1ARB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_lyticus Achromobacter lyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARB OCA]. |
==Reference== | ==Reference== | ||
| - | The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease., Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F, J Biol Chem. 1989 Mar 5;264(7):3832-9. PMID:[http:// | + | The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease., Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F, J Biol Chem. 1989 Mar 5;264(7):3832-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2492988 2492988] |
[[Category: Achromobacter lyticus]] | [[Category: Achromobacter lyticus]] | ||
[[Category: Lysyl endopeptidase]] | [[Category: Lysyl endopeptidase]] | ||
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[[Category: hydrolase(serine protease)]] | [[Category: hydrolase(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 10:01:20 2008'' |
Revision as of 08:01, 20 March 2008
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| , resolution 1.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Lysyl endopeptidase, with EC number 3.4.21.50 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE
Overview
The complete amino acid sequence of Achromobacter lyticus protease I (EC 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been established. This has been achieved by sequence analysis of the reduced and S-carboxymethylated protease and of peptides obtained by enzymatic digestion with Achromobacter protease I itself and Staphylococcus aureus V8 protease and by chemical cleavage with cyanogen bromide. The protease consists of 268 residues with three disulfide bonds, which have been assigned to Cys6-Cys216, Cys12-Cys80, and Cys36-Cys58. Comparison of the amino acid sequence of Achromobacter protease and other serine proteases of bacterial and mammalian origins has revealed that Achromobacter protease I is a mammalian-type serine protease of which the catalytic triad comprises His57, Asp113, and Ser194. It has also been shown that the protease has 9- and 26-residue extensions of the peptide chain at the N and C termini, respectively, and overall sequence homology is as low as 20% with bovine trypsin. The presence of a disulfide bridge between the N-terminal extension Cys6 and Cys216 close to the putative active site in the C-terminal region is thought to be responsible for the generation of maximal proteolytic function in the pH range 8.5-10.7 and enhanced stability to denaturation.
About this Structure
1ARB is a Single protein structure of sequence from Achromobacter lyticus. Full crystallographic information is available from OCA.
Reference
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease., Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F, J Biol Chem. 1989 Mar 5;264(7):3832-9. PMID:2492988
Page seeded by OCA on Thu Mar 20 10:01:20 2008
