1dyz

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[[Image:1dyz.gif|left|200px]]
 
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==OXIDISED AZURIN II FROM ALCALIGENES XYLOSOXIDANS==
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The line below this paragraph, containing "STRUCTURE_1dyz", creates the "Structure Box" on the page.
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<StructureSection load='1dyz' size='340' side='right'caption='[[1dyz]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1dyz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1arn 1arn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DYZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.75&#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></td></tr>
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{{STRUCTURE_1dyz| PDB=1dyz | SCENE= }}
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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=1dyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyz OCA], [https://pdbe.org/1dyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dyz RCSB], [https://www.ebi.ac.uk/pdbsum/1dyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dyz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZUR2_ALCXX AZUR2_ALCXX] 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/dy/1dyz_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=1dyz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A resolution. Data were collected using one crystal in each case and by translating the crystal after each oscillation range to minimize photoreduction. Very small differences are observed at the Cu site upon reduction and these cannot be determined with confidence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for Cu-His46, where a larger deviation of approximately 0.12-0.18 A is observed, indicating that this ligand is more tightly restrained in the crystallographic refinement at the current resolution.
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'''OXIDISED AZURIN II FROM ALCALIGENES XYLOSOXIDANS'''
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Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 A resolution.,Dodd FE, Abraham ZH, Eady RR, Hasnain SS Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):690-6. PMID:10818345<ref>PMID:10818345</ref>
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==Overview==
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Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A resolution. Data were collected using one crystal in each case and by translating the crystal after each oscillation range to minimize photoreduction. Very small differences are observed at the Cu site upon reduction and these cannot be determined with confidence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for Cu-His46, where a larger deviation of approximately 0.12-0.18 A is observed, indicating that this ligand is more tightly restrained in the crystallographic refinement at the current resolution.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1DYZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1arn 1arn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYZ OCA].
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</div>
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<div class="pdbe-citations 1dyz" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 A resolution., Dodd FE, Abraham ZH, Eady RR, Hasnain SS, Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):690-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10818345 10818345]
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*[[Azurin 3D structures|Azurin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Abraham, Z H.L.]]
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[[Category: Abraham ZHL]]
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[[Category: Dodd, F E.]]
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[[Category: Dodd FE]]
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[[Category: Eady, R R.]]
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[[Category: Eady RR]]
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[[Category: Hasnain, S S.]]
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[[Category: Hasnain SS]]
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[[Category: Copper]]
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[[Category: Cupredoxin]]
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[[Category: Electron transport]]
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[[Category: Periplasmic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:27:02 2008''
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Current revision

OXIDISED AZURIN II FROM ALCALIGENES XYLOSOXIDANS

PDB ID 1dyz

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