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1gr7

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Revision as of 06:30, 3 January 2018

Crystal structure of the double mutant Cys3Ser/Ser100Pro from Pseudomonas Aeruginosa at 1.8 A resolution

Structural highlights

1gr7 is a 4 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1ag0, 1azn, 1azr, 1azu, 1bex, 1cc3, 1e5y, 1e5z, 1e65, 1e67, 1etj, 1ezl, 1i53, 1ils, 1ilu, 1jze, 1jzf, 1jzg, 1jzh, 1jzi, 1jzj, 1nzr, 1vlx, 2azu, 2tsa, 2tsb, 3azu, 4azu, 5azu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.

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

Azurin is a cupredoxin, which functions as an electron carrier. Its fold is dominated by a beta-sheet structure. In the present study, azurin serves as a model system to investigate the importance of a conserved disulphide bond for protein stability and folding/unfolding. For this purpose, we have examined two azurin mutants, the single mutant Cys3Ser, which disrupts azurin's conserved disulphide bond, and the double mutant Cys3Ser/Ser100Pro, which contains an additional mutation at a site distant from the conserved disulphide. The crystal structure of the azurin double mutant has been determined to 1.8 A resolution(2), with a crystallographic R-factor of 17.5% (R(free)=20.8%). A comparison with the wild-type structure reveals that structural differences are limited to the sites of the mutations. Also, the rates of folding and unfolding as determined by CD and fluorescence spectroscopy are almost unchanged. The main difference to wild-type azurin is a destabilisation by approximately 20 kJ x mol(-1), constituting half the total folding energy of the wild-type protein. Thus, the disulphide bond constitutes a vital component in giving azurin its stable fold.

Crystal structure of the double azurin mutant Cys3Ser/Ser100Pro from Pseudomonas aeruginosa at 1.8 A resolution: its folding-unfolding energy and unfolding kinetics.,Okvist M, Bonander N, Sandberg A, Karlsson BG, Krengel U, Xue Y, Sjolin L Biochim Biophys Acta. 2002 Apr 29;1596(2):336-45. PMID:12007613^[1]

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

References

↑ Okvist M, Bonander N, Sandberg A, Karlsson BG, Krengel U, Xue Y, Sjolin L. Crystal structure of the double azurin mutant Cys3Ser/Ser100Pro from Pseudomonas aeruginosa at 1.8 A resolution: its folding-unfolding energy and unfolding kinetics. Biochim Biophys Acta. 2002 Apr 29;1596(2):336-45. PMID:12007613

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gr7"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE DOUBLE MUTANT CYS3SER/SER100PRO FROM PSEUDOMONAS AERUGINOSA AT 1.8 A RESOLUTION==
+==Crystal structure of the double mutant Cys3Ser/Ser100Pro from Pseudomonas Aeruginosa at 1.8 A resolution==
 <StructureSection load='1gr7' size='340' side='right' caption='[[1gr7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ag0|1ag0]], [[1azn|1azn]], [[1azr|1azr]], [[1azu|1azu]], [[1bex|1bex]], [[1cc3|1cc3]], [[1e5y|1e5y]], [[1e5z|1e5z]], [[1e65|1e65]], [[1e67|1e67]], [[1etj|1etj]], [[1ezl|1ezl]], [[1i53|1i53]], [[1ils|1ils]], [[1ilu|1ilu]], [[1jze|1jze]], [[1jzf|1jzf]], [[1jzg|1jzg]], [[1jzh|1jzh]], [[1jzi|1jzi]], [[1jzj|1jzj]], [[1nzr|1nzr]], [[1vlx|1vlx]], [[2azu|2azu]], [[2tsa|2tsa]], [[2tsb|2tsb]], [[3azu|3azu]], [[4azu|4azu]], [[5azu|5azu]]</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=1gr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gr7 OCA], [http://pdbe.org/1gr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gr7 RCSB], [http://www.ebi.ac.uk/pdbsum/1gr7 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=1gr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gr7 OCA], [http://pdbe.org/1gr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gr7 RCSB], [http://www.ebi.ac.uk/pdbsum/1gr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gr7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/1gr7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/1gr7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1gr7" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Azurin|Azurin]]
 == References ==
 <references/>

1gr7

From Proteopedia

Revision as of 06:30, 3 January 2018

Crystal structure of the double mutant Cys3Ser/Ser100Pro from Pseudomonas Aeruginosa at 1.8 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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