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1bqk

From Proteopedia

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OXIDIZED PSEUDOAZURIN

Structural highlights

1bqk is a 1 chain structure with sequence from Achromobacter cycloclastes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.35Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Inoue T, Nishio N, Suzuki S, Kataoka K, Kohzuma T, Kai Y. 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. J Biol Chem. 1999 Jun 18;274(25):17845-52. PMID:10364229

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bqk"

@@ Line 4: / Line 4: @@
 == 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='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>
+</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.
+[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]]
@@ Line 37: / Line 38: @@
 [[Category: Achromobacter cycloclastes]]
 [[Category: Large Structures]]
-[[Category: Hamanaka, S]]
+[[Category: Hamanaka S]]
-[[Category: Harada, S]]
+[[Category: Harada S]]
-[[Category: Inoue, T]]
+[[Category: Inoue T]]
-[[Category: Iwasaki, H]]
+[[Category: Iwasaki H]]
-[[Category: Kai, Y]]
+[[Category: Kai Y]]
-[[Category: Kohzuma, T]]
+[[Category: Kohzuma T]]
-[[Category: Nishio, N]]
+[[Category: Nishio N]]
-[[Category: Shidara, S]]
+[[Category: Shidara S]]
-[[Category: Shimomura, T]]
+[[Category: Shimomura T]]
-[[Category: Suzuki, S]]
+[[Category: Suzuki S]]
-[[Category: Cuproprotein]]
-[[Category: Electron transport]]

1bqk

From Proteopedia

Current revision

OXIDIZED PSEUDOAZURIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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