1arc
From Proteopedia
(New page: 200px<br /><applet load="1arc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1arc, resolution 2.0Å" /> '''THE PRIMARY STRUCTURE...) |
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| - | [[Image:1arc.gif|left|200px]]<br /><applet load="1arc" size=" | + | [[Image:1arc.gif|left|200px]]<br /><applet load="1arc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1arc, resolution 2.0Å" /> | caption="1arc, resolution 2.0Å" /> | ||
'''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE'''<br /> | '''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The complete amino acid sequence of Achromobacter lyticus protease I (EC | + | 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== | ==About this Structure== | ||
| - | 1ARC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_lyticus Achromobacter lyticus] with TCK as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1ARC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_lyticus Achromobacter lyticus] with <scene name='pdbligand=TCK:'>TCK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase(serine protease)]] | [[Category: hydrolase(serine protease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:29 2008'' |
Revision as of 09:47, 21 February 2008
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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
1ARC is a Single protein structure of sequence from Achromobacter lyticus with as ligand. Active as Lysyl endopeptidase, with EC number 3.4.21.50 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
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