1bqk: Difference between revisions
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New page: left|200px<br /> <applet load="1bqk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqk, resolution 1.35Å" /> '''OXIDIZED PSEUDOAZUR... |
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== | ==OXIDIZED PSEUDOAZURIN== | ||
The crystal structures of oxidized and reduced pseudoazurins from a | <StructureSection load='1bqk' size='340' side='right'caption='[[1bqk]], [[Resolution|resolution]] 1.35Å' 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]] 1.35Å</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1bqk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Pseudoazurin|Pseudoazurin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Achromobacter cycloclastes]] | [[Category: Achromobacter cycloclastes]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hamanaka | [[Category: Hamanaka S]] | ||
[[Category: Harada | [[Category: Harada S]] | ||
[[Category: Inoue | [[Category: Inoue T]] | ||
[[Category: Iwasaki | [[Category: Iwasaki H]] | ||
[[Category: Kai | [[Category: Kai Y]] | ||
[[Category: Kohzuma | [[Category: Kohzuma T]] | ||
[[Category: Nishio | [[Category: Nishio N]] | ||
[[Category: Shidara | [[Category: Shidara S]] | ||
[[Category: Shimomura | [[Category: Shimomura T]] | ||
[[Category: Suzuki | [[Category: Suzuki S]] | ||
