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1azb

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(New page: 200px<br /><applet load="1azb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azb, resolution 2.2&Aring;" /> '''STRUCTURE OF APO-AZUR...)
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[[Image:1azb.gif|left|200px]]<br /><applet load="1azb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1azb, resolution 2.2&Aring;" />
 
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'''STRUCTURE OF APO-AZURIN FROM ALCALIGENES DENITRIFICANS AT 1.8 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==STRUCTURE OF APO-AZURIN FROM ALCALIGENES DENITRIFICANS AT 1.8 ANGSTROMS RESOLUTION==
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The structure of apo-azurin from Alcaligenes denitrificans has been, determined at high resolution by X-ray crystallography. Two separate, structure analyses have been carried out, (i) on crystals obtained from, solutions of apo-azurin and (ii) on crystals obtained by removal of copper, from previously formed crystals of holo-azurin. Data to 1.8 A resolution, were collected from the apo-azurin crystals, by Weissenberg photography, (with image plates) using synchrotron radiation and by diffractometry, and, the structure was refined by restrained least-squares methods to a final R, value of 0.160 for all data in the range 10.0-1.8 A. The final model of, 1954 protein atoms, 246 water molecules (66 half-weighted), four SO(4)(2-), ions, and two low-occupancy (0.13 and 0.15) Cu atoms has r.m.s. deviations, of 0.012, 0.045 and 0.013 A from standard bond lengths, angle distances, and planar groups. For copper-removed azurin, data to 2.2 A were collected, by diffractometry and the structure refined by restrained least squares to, a final R value of 0.158 for all data in the range 10.0-2.2 A. The final, model of 1954 protein atoms, 264 water molecules, two SO(4)(2-) ions, two, low occupancy (0.18 and 0.22) metal atoms and one unidentified atom, (modelled as S) has r.m.s. deviations of 0.013, 0.047 and 0.012 A from, standard bond lengths, angle distances and planar groups. The two, structures are essentially identical to each other and show no significant, differences from the oxidized and reduced holo-azurin structures. The, ligand side chains move slightly closer together following the removal of, copper, with the radius of the cavity between the three strongly binding, ligands, His 46, His 117 and Cys 112, shrinking from 1.31 A in reduced, azurin to 1.24 A in oxidized azurin and 1.16 A in apo-azurin. There is a, suggestion of increased flexibility in one of the copper-binding loops but, the structure supports the view that the copper site found in holo-azurin, is a stable structure, defined by the constraints of the polypeptide, structure even in the absence of a bound metal ion.
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<StructureSection load='1azb' size='340' side='right'caption='[[1azb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1azb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AZB FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1azb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azb OCA], [https://pdbe.org/1azb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azb RCSB], [https://www.ebi.ac.uk/pdbsum/1azb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZUR_ACHDE AZUR_ACHDE] 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/az/1azb_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=1azb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AZB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans] with CU and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AZB OCA].
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*[[Azurin 3D structures|Azurin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of apo-azurin from Alcaligenes denitrificans at 1.8 A resolution., Shepard WE, Kingston RL, Anderson BF, Baker EN, Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):331-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299522 15299522]
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[[Category: Achromobacter xylosoxidans]]
[[Category: Achromobacter xylosoxidans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baker, E.N.]]
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[[Category: Baker EN]]
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[[Category: Shepard, W.E.B.]]
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[[Category: Shepard WEB]]
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[[Category: CU]]
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[[Category: SO4]]
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[[Category: electron transport(copper)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:13:16 2007''
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Current revision

STRUCTURE OF APO-AZURIN FROM ALCALIGENES DENITRIFICANS AT 1.8 ANGSTROMS RESOLUTION

PDB ID 1azb

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