This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1arc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1arc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1arc, resolution 2.0&Aring;" /> '''THE PRIMARY STRUCTURE...)
Current revision (15:27, 13 March 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1arc.gif|left|200px]]<br /><applet load="1arc" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1arc, resolution 2.0&Aring;" />
 
-
'''THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE'''<br />
 
-
==Overview==
+
==THE PRIMARY STRUCTURE AND STRUCTURAL CHARACTERISTICS OF ACHROMOBACTER LYTICUS PROTEASE I, A LYSINE-SPECIFIC SERINE PROTEASE==
-
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.
+
<StructureSection load='1arc' size='340' side='right'caption='[[1arc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<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>
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ARC OCA].
+
</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>
-
 
+
<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>
-
==Reference==
+
<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>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=2492988 2492988]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/API_ACHLY API_ACHLY]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/1arc_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Achromobacter lyticus]]
[[Category: Achromobacter lyticus]]
-
[[Category: Lysyl endopeptidase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Katsube Y]]
-
[[Category: Katsube, Y.]]
+
[[Category: Kitagawa Y]]
-
[[Category: Kitagawa, Y.]]
+
-
[[Category: TCK]]
+
-
[[Category: hydrolase(serine protease)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:04:10 2007''
+

Current revision

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

PDB ID 1arc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1arc"
Personal tools