1cur
From Proteopedia
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| - | [[Image:1cur.gif|left|200px]] | + | [[Image:1cur.gif|left|200px]] |
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| - | '''REDUCED RUSTICYANIN, NMR''' | + | {{Structure |
| + | |PDB= 1cur |SIZE=350|CAPTION= <scene name='initialview01'>1cur</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REDUCED RUSTICYANIN, NMR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CUR is a [ | + | 1CUR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUR OCA]. |
==Reference== | ==Reference== | ||
| - | NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential., Botuyan MV, Toy-Palmer A, Chung J, Blake RC 2nd, Beroza P, Case DA, Dyson HJ, J Mol Biol. 1996 Nov 15;263(5):752-67. PMID:[http:// | + | NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential., Botuyan MV, Toy-Palmer A, Chung J, Blake RC 2nd, Beroza P, Case DA, Dyson HJ, J Mol Biol. 1996 Nov 15;263(5):752-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8947573 8947573] |
[[Category: Acidithiobacillus ferrooxidans]] | [[Category: Acidithiobacillus ferrooxidans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: type 1 copper protein]] | [[Category: type 1 copper protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:09 2008'' |
Revision as of 08:29, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDUCED RUSTICYANIN, NMR
Overview
The solution structure of the Cu(I) form of the rusticyanin from Thiobacillus ferrooxidans has been calculated from a total of 1979 distance and dihedral angle constraints derived from 1H, 13C and 15N NMR spectra. The structures reveal two beta-sheets, one of six strands and one of seven strands that are tightly packed in a beta-barrel or beta-sandwich arrangement, and a short helix that extends on the outside of one of the sheets to form a second hydrophobic core. The copper coordination sphere is composed of the standard type I ligands (His2CysMet) in a distorted tetrahedral arrangement. The copper-binding site is located within a hydrophobic region at one end of the molecule, surrounded by a number of aromatic rings and hydrophobic residues. This configuration probably contributes to the acid stability of the copper site, since close association of the aromatic rings with the histidine ligands would sterically hinder their dissociation from the copper. An electrostatic analysis based on a comparison of the structures of rusticyanin and French bean plastocyanin shows that factors determining the high redox potential of rusticyanin include contributions from charged side-chains and from the disposition of backbone peptide dipoles, particularly in the 81 to 86 region of the sequence and the ligand cysteine residue. These interactions should also contribute to the acid stability by inhibiting protonation of His143.
About this Structure
1CUR is a Single protein structure of sequence from Acidithiobacillus ferrooxidans. Full crystallographic information is available from OCA.
Reference
NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential., Botuyan MV, Toy-Palmer A, Chung J, Blake RC 2nd, Beroza P, Case DA, Dyson HJ, J Mol Biol. 1996 Nov 15;263(5):752-67. PMID:8947573
Page seeded by OCA on Thu Mar 20 10:29:09 2008
