1bqr
From Proteopedia
(Difference between revisions)
(9 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:1bqr.png|left|200px]] | ||
- | + | ==REDUCED PSEUDOAZURIN== | |
+ | <StructureSection load='1bqr' size='340' side='right'caption='[[1bqr]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1bqr]] 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=1BQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQR 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]] 1.6Å</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=1bqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqr OCA], [https://pdbe.org/1bqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqr RCSB], [https://www.ebi.ac.uk/pdbsum/1bqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqr 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/1bqr_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=1bqr 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 1bqr" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Pseudoazurin|Pseudoazurin]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Achromobacter cycloclastes]] | [[Category: Achromobacter cycloclastes]] | ||
- | [[Category: Hamanaka | + | [[Category: Large Structures]] |
- | [[Category: Harada | + | [[Category: Hamanaka S]] |
- | [[Category: Inoue | + | [[Category: Harada S]] |
- | [[Category: Iwasaki | + | [[Category: Inoue T]] |
- | [[Category: Kai | + | [[Category: Iwasaki H]] |
- | [[Category: Kohzuma | + | [[Category: Kai Y]] |
- | [[Category: Nishio | + | [[Category: Kohzuma T]] |
- | [[Category: Shidara | + | [[Category: Nishio N]] |
- | [[Category: Shimomura | + | [[Category: Shidara S]] |
- | [[Category: Suzuki | + | [[Category: Shimomura T]] |
- | + | [[Category: Suzuki S]] | |
- | + |
Current revision
REDUCED PSEUDOAZURIN
|
Categories: Achromobacter cycloclastes | Large Structures | Hamanaka S | Harada S | Inoue T | Iwasaki H | Kai Y | Kohzuma T | Nishio N | Shidara S | Shimomura T | Suzuki S