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1vlx

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[[Image:1vlx.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF ELECTRON TRANSFER (COBALT-PROTEIN)==
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|PDB= 1vlx |SIZE=350|CAPTION= <scene name='initialview01'>1vlx</scene>, resolution 1.9&Aring;
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<StructureSection load='1vlx' size='340' side='right'caption='[[1vlx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
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<table><tr><td colspan='2'>[[1vlx]] 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=1VLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLX FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
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|DOMAIN=
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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=1vlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlx OCA], [https://pdbe.org/1vlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlx RCSB], [https://www.ebi.ac.uk/pdbsum/1vlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlx ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlx OCA], [http://www.ebi.ac.uk/pdbsum/1vlx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vlx RCSB]</span>
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== Function ==
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}}
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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/vl/1vlx_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=1vlx ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF ELECTRON TRANSFER (COBALT-PROTEIN)'''
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==See Also==
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*[[Azurin 3D structures|Azurin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of cobalt-substituted azurin from Pseudomonas aeruginosa has been determined to final crystallographic R value of 0.175 at 1.9 A resolution. There are four molecules in the asymmetric unit in the structure, and these four molecules are packed as a dimer of dimers. The dimer packing is very similar to that of the wild-type Pseudomonas aeruginosa azurin dimer. Replacement of the native copper by the cobalt ion has only small effects on the metal binding site presumably because of the existence of an extensive network of hydrogen bonds in its immediate neighborhood. Some differences are obvious, however. In wild-type azurin the copper atom occupies a distorted trigonal bipyramidal site, while cobalt similar to zinc and nickel occupy a distorted tetrahedral site, in which the distance to the Met121,S(delta) atom is increased to 3.3-3.5 A and the distance to the carbonyl oxygen of Gly45 has decreased to 2.1-2.4 A. The X-band EPR spectrum of the high-spin Co(II) in azurin is well resolved (apparent g values gx' = 5.23; gy' = 3.83; gz' = 1.995, and hyperfine splittings Ax' = 31; Ay' = 20-30; Az' = 53 G) and indicates that the ligand field is close to axial.
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[[Category: Large Structures]]
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==About this Structure==
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1VLX 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=1VLX OCA].
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==Reference==
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The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and Co-EPR spectroscopy., Bonander N, Vanngard T, Tsai LC, Langer V, Nar H, Sjolin L, Proteins. 1997 Mar;27(3):385-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9094740 9094740]
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[[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: Langer V]]
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[[Category: Langer, V.]]
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[[Category: Nar H]]
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[[Category: Nar, H.]]
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[[Category: Sjolin L]]
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[[Category: Sjolin, L.]]
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[[Category: Tsai L-C]]
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[[Category: Tsai, L C.]]
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[[Category: Vanngard T]]
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[[Category: Vanngard, T.]]
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[[Category: copper]]
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[[Category: electron transport]]
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[[Category: periplasmic]]
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[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:26:12 2008''
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Current revision

STRUCTURE OF ELECTRON TRANSFER (COBALT-PROTEIN)

PDB ID 1vlx

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