1jvl: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jvl]] is a 2 chain structure with 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=1JVL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JVL FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jvl]] is a 2 chain structure with 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=1JVL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JVL FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jvl RCSB], [http://www.ebi.ac.uk/pdbsum/1jvl 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=1jvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jvl RCSB], [http://www.ebi.ac.uk/pdbsum/1jvl PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Amsterdam, I M.C van | [[Category: Amsterdam, I M.C van]] | ||
[[Category: Canters, G W | [[Category: Canters, G W]] | ||
[[Category: Cavazzini, D | [[Category: Cavazzini, D]] | ||
[[Category: Einsle, O | [[Category: Einsle, O]] | ||
[[Category: Merli, A | [[Category: Merli, A]] | ||
[[Category: Messerschmidt, A | [[Category: Messerschmidt, A]] | ||
[[Category: Rossi, G L | [[Category: Rossi, G L]] | ||
[[Category: Ubbink, M | [[Category: Ubbink, M]] | ||
[[Category: Covalent crosslink]] | [[Category: Covalent crosslink]] | ||
[[Category: Cupredoxin]] | [[Category: Cupredoxin]] | ||
[[Category: Electron transfer]] | [[Category: Electron transfer]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
Revision as of 17:45, 25 December 2014
Azurin dimer, covalently crosslinked through bis-maleimidomethyletherAzurin dimer, covalently crosslinked through bis-maleimidomethylether
Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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