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1ezl

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(New page: 200px<br /><applet load="1ezl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ezl, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ezl.jpg|left|200px]]<br /><applet load="1ezl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ezl, resolution 2.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND STABILITY?'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND STABILITY?==
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Azurin has a beta-barrel fold comprising eight beta-strands and one alpha, helix. A disulfide bond between residues 3 and 26 connects the N-termini, of beta strands beta1 and beta3. Three mutant proteins lacking the, disulfide bond were constructed, C3A/C26A, C3A/C26I and a putative salt, bridge (SB) in the C3A/S25R/C26A/K27R mutant. All three mutants exhibit, spectroscopic properties similar to the wild-type protein. Furthermore, the crystal structure of the C3A/C26A mutant was determined at 2.0 A, resolution and, in comparison to the wild-type protein, the only, differences are found in the immediate proximity of the mutation. The, mutants lose the 628 nm charge-transfer band at a temperature 10-22, degrees C lower than the wild-type protein. The folding of the zinc loaded, C3A/C26A mutant was studied by guanidine hydrochloride (GdnHCl) induced, denaturation monitored both by fluorescence and CD spectroscopy. The, midpoint in the folding equilibrium, at 1.3 M GdnHCl, was observed using, both CD and fluorescence spectroscopy. The free energy of folding, determined from CD is -24.9 kJ.mol-1, a destabilization of approximately, 20 kJ.mol-1 compared to the wild-type Zn2+-protein carrying an intact, disulfide bond, indicating that the disulfide bond is important for giving, azurin its stable structure. The C3A/C26I mutant is more stable and the SB, mutant is less stable than C3A/C26A, both in terms of folding energy and, thermal denaturation. The folding intermediate of the wild-type, Zn2+-azurin is not observed for the disulfide-deficient C3A/C26A mutant., The rate of unfolding for the C3A/C26A mutant is similar to that of the, wild-type protein, suggesting that the site of the mutation is not, involved in an early unfolding reaction.
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<StructureSection load='1ezl' size='340' side='right'caption='[[1ezl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ezl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EZL FirstGlance]. <br>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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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=1ezl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezl OCA], [https://pdbe.org/1ezl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ezl RCSB], [https://www.ebi.ac.uk/pdbsum/1ezl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ezl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/1ezl_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1ezl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EZL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EZL OCA].
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*[[Azurin 3D structures|Azurin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond for folding and stability?, Bonander N, Leckner J, Guo H, Karlsson BG, Sjolin L, Eur J Biochem. 2000 Jul;267(14):4511-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10880975 10880975]
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Bonander N]]
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[[Category: Bonander, N.]]
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[[Category: Guo H]]
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[[Category: Guo, H.]]
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[[Category: Karlsson BG]]
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[[Category: Karlsson, B.G.]]
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[[Category: Leckner J]]
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[[Category: Leckner, J.]]
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[[Category: Sjolin L]]
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[[Category: Sjolin, L.]]
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[[Category: CU]]
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[[Category: crystal structure]]
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[[Category: disulphide bond]]
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[[Category: greek key fold]]
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[[Category: mutant]]
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[[Category: protein folding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:28:09 2007''
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Current revision

CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND STABILITY?

PDB ID 1ezl

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