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1jvl

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Azurin dimer, covalently crosslinked through bis-maleimidomethylether

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

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-[[Image:1jvl.gif|left|200px]]<br /><applet load="1jvl" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jvl, resolution 2.0&Aring;" />
-'''Azurin dimer, covalently crosslinked through bis-maleimidomethylether'''<br />
-==Overview==
+==Azurin dimer, covalently crosslinked through bis-maleimidomethylether==
-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.
+<StructureSection load='1jvl' size='340' side='right'caption='[[1jvl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jvl]] is a 2 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=1JVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVL 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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OPP:1-[PYRROL-1-YL-2,5-DIONE-METHOXYMETHYL]-PYRROLE-2,5-DIONE'>OPP</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=1jvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvl OCA], [https://pdbe.org/1jvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvl RCSB], [https://www.ebi.ac.uk/pdbsum/1jvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvl 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/1jvl_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=1jvl ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-JVL 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, NI, 144 and OPP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JVL OCA].
+*[[Azurin 3D structures|Azurin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11740504 11740504]
+[[Category: Large Structures]]
 [[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: 144]]
-[[Category: CU]]
-[[Category: NI]]
-[[Category: OPP]]
-[[Category: covalent crosslink]]
-[[Category: cupredoxin]]
-[[Category: electron transfer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:36:41 2007''

1jvl

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Azurin dimer, covalently crosslinked through bis-maleimidomethylether

Structural highlights

Function

Evolutionary Conservation

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