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2c0y

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Revision as of 08:00, 23 May 2018

THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S

Structural highlights

2c0y is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1bxf, 1glo, 1ms6, 1npz, 1nqc
Activity:	Cathepsin S, with EC number 3.4.22.27
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the active-site mutant Cys25 --> Ala of glycosylated human procathepsin S is reported. It was determined by molecular replacement and refined to 2.1 Angstrom resolution, with an R-factor of 0.198. The overall structure is very similar to other cathepsin L-like zymogens of the C1A clan. The peptidase unit comprises two globular domains, and a small third domain is formed by the N-terminal part of the prosequence. It is anchored to the prosegment binding loop of the enzyme. Prosegment residues beyond the prodomain dock to the substrate binding cleft in a nonproductive orientation. Structural comparison with published data for mature cathepsin S revealed that procathepsin S residues Phe146, Phe70, and Phe211 adopt different orientations. Being part of the S1' and S2 pockets, they may contribute to the selectivity of ligand binding. Regarding the prosequence, length, orientation and anchoring of helix alpha3p differ from related zymogens, thereby possibly contributing to the specificity of propeptide-enzyme interaction in the papain family. The discussion focuses on the functional importance of the most conserved residues in the prosequence for structural integrity, inhibition and folding assistance, considering scanning mutagenesis data published for procathepsin S and for its isolated propeptide.

The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.,Kaulmann G, Palm GJ, Schilling K, Hilgenfeld R, Wiederanders B Protein Sci. 2006 Nov;15(11):2619-29. PMID:17075137^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kaulmann G, Palm GJ, Schilling K, Hilgenfeld R, Wiederanders B. The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions. Protein Sci. 2006 Nov;15(11):2619-29. PMID:17075137 doi:15/11/2619

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c0y"

@@ Line 1: / Line 1: @@
 ==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==
 <StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bxf|1bxf]], [[1glo|1glo]], [[1ms6|1ms6]], [[1npz|1npz]], [[1nqc|1nqc]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://pdbe.org/2c0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://pdbe.org/2c0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c0y_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c0y_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2c0y ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2c0y

From Proteopedia

Revision as of 08:00, 23 May 2018

THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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