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1arc

From Proteopedia

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[[Image:1arc.gif|left|200px]]
 
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{{Structure
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==THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE==
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|PDB= 1arc |SIZE=350|CAPTION= <scene name='initialview01'>1arc</scene>, resolution 2.0&Aring;
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<StructureSection load='1arc' size='340' side='right'caption='[[1arc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=TCK:N-TOSYL-L-LYSINYL+METHYL+KETONE'>TCK</scene>
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<table><tr><td colspan='2'>[[1arc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_lyticus Achromobacter lyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ARC FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TCK:N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-METHYLBENZENESULFONAMIDE'>TCK</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1arc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arc OCA], [https://pdbe.org/1arc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1arc RCSB], [https://www.ebi.ac.uk/pdbsum/1arc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1arc ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1arc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arc OCA], [http://www.ebi.ac.uk/pdbsum/1arc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1arc RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/API_ACHLY API_ACHLY]
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== Evolutionary Conservation ==
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'''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/1arc_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1ARC 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=1ARC OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1arc ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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]
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</StructureSection>
[[Category: Achromobacter lyticus]]
[[Category: Achromobacter lyticus]]
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[[Category: Lysyl endopeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Katsube Y]]
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[[Category: Katsube, Y.]]
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[[Category: Kitagawa Y]]
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[[Category: Kitagawa, Y.]]
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[[Category: hydrolase(serine protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:05 2008''
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Current revision

THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE

PDB ID 1arc

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