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[[Image:1jvo.gif|left|200px]]
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{{STRUCTURE_1jvo|  PDB=1jvo  |  SCENE=  }}
'''Azurin dimer, crosslinked via disulfide bridge'''


==Azurin dimer, crosslinked via disulfide bridge==
<StructureSection load='1jvo' size='340' side='right'caption='[[1jvo]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jvo]] is a 12 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=1JVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvo OCA], [https://pdbe.org/1jvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvo RCSB], [https://www.ebi.ac.uk/pdbsum/1jvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
== 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/jv/1jvo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1jvo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.


==Overview==
Dramatic modulation of electron transfer in protein complexes by crosslinking.,van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:11740504<ref>PMID:11740504</ref>
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JVO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVO OCA].
</div>
<div class="pdbe-citations 1jvo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Dramatic modulation of electron transfer in protein complexes by crosslinking., van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW, Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11740504 11740504]
*[[Azurin 3D structures|Azurin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Canters GW]]
[[Category: Amsterdam, I M.C van.]]
[[Category: Cavazzini D]]
[[Category: Canters, G W.]]
[[Category: Einsle O]]
[[Category: Cavazzini, D.]]
[[Category: Merli A]]
[[Category: Einsle, O.]]
[[Category: Messerschmidt A]]
[[Category: Merli, A.]]
[[Category: Rossi GL]]
[[Category: Messerschmidt, A.]]
[[Category: Ubbink M]]
[[Category: Rossi, G L.]]
[[Category: Van Amsterdam IMC]]
[[Category: Ubbink, M.]]
[[Category: Covalent crosslink]]
[[Category: Cupredoxin]]
[[Category: Electron transfer]]
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