1jvl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1jvl' size='340' side='right'caption='[[1jvl]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1jvl' size='340' side='right'caption='[[1jvl]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1jvl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | <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> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1jvl 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=1jvl ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
- | |||
- | 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> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1jvl" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Azurin 3D structures|Azurin 3D structures]] | *[[Azurin 3D structures|Azurin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Pseudomonas aeruginosa]] |
- | [[Category: Canters | + | [[Category: Canters GW]] |
- | [[Category: Cavazzini | + | [[Category: Cavazzini D]] |
- | [[Category: Einsle | + | [[Category: Einsle O]] |
- | [[Category: Merli | + | [[Category: Merli A]] |
- | [[Category: Messerschmidt | + | [[Category: Messerschmidt A]] |
- | [[Category: Rossi | + | [[Category: Rossi GL]] |
- | [[Category: Ubbink | + | [[Category: Ubbink M]] |
- | [[Category: | + | [[Category: Van Amsterdam IMC]] |
- | + | ||
- | + | ||
- | + |
Revision as of 07:55, 3 April 2024
Azurin dimer, covalently crosslinked through bis-maleimidomethylether
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