View source for 1bqk


==OXIDIZED PSEUDOAZURIN==
<StructureSection load='1bqk' size='340' side='right'caption='[[1bqk]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bqk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqk OCA], [https://pdbe.org/1bqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqk RCSB], [https://www.ebi.ac.uk/pdbsum/1bqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AZUP_ACHCY AZUP_ACHCY] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/1bqk_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1bqk ConSurf].
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== Publication Abstract from PubMed ==
The crystal structures of oxidized and reduced pseudoazurins from a denitrifying bacterium, Achromobacter cycloclastes IAM1013, have been determined at 1.35- and 1.6-A resolutions, respectively. The copper site in the oxidized state exhibits a distorted tetrahedral structure like those of other pseudoazurins. However, not only a small change of the copper geometry, but concerted peptide bond flips are identified. The imidazole ring of remote His6 has a hydrogen bonding distance of 2.73 A between N-delta1(His6) and O-gamma1(Thr36) in the oxidized protein. When the protein is reduced at pH 6.0, the imidazole ring rotates by 30.3 degrees and moves 1.00 A away from the position of the oxidized state. A new hydrogen bond between N-epsilon2(His6) and O-epsilon1(Glu4) is formed with a distance of 3.03 A, while the hydrogen bond between N-delta1(His6)-O-gamma1(Thr36) is maintained with an interatomic distance of 2.81 A. A concomitant peptide bond flip of main chain between Ile34 and Thr36 occurs.

Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine.,Inoue T, Nishio N, Suzuki S, Kataoka K, Kohzuma T, Kai Y J Biol Chem. 1999 Jun 18;274(25):17845-52. PMID:10364229<ref>PMID:10364229</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1bqk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pseudoazurin|Pseudoazurin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Achromobacter cycloclastes]]
[[Category: Large Structures]]
[[Category: Hamanaka S]]
[[Category: Harada S]]
[[Category: Inoue T]]
[[Category: Iwasaki H]]
[[Category: Kai Y]]
[[Category: Kohzuma T]]
[[Category: Nishio N]]
[[Category: Shidara S]]
[[Category: Shimomura T]]
[[Category: Suzuki S]]