1bqr
From Proteopedia
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| - | [[Image:1bqr.gif|left|200px]]<br /><applet load="1bqr" size=" | + | [[Image:1bqr.gif|left|200px]]<br /><applet load="1bqr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bqr, resolution 1.6Å" /> | caption="1bqr, resolution 1.6Å" /> | ||
'''REDUCED PSEUDOAZURIN'''<br /> | '''REDUCED PSEUDOAZURIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=COP:Reduced Cu Coordination'>COP</scene>. Full crystallographic information is available from [http:// | + | 1BQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=COP:Reduced+Cu+Coordination'>COP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:33:40 2008'' |
Revision as of 07:33, 3 February 2008
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REDUCED PSEUDOAZURIN
Overview
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.
About this Structure
1BQR is a Single protein structure of sequence from Achromobacter cycloclastes with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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