1cur: Difference between revisions

Revision as of 21:24, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cur.png

Template:STRUCTURE 1cur

REDUCED RUSTICYANIN, NMRREDUCED RUSTICYANIN, NMR

Template:ABSTRACT PUBMED 8947573

About this StructureAbout this Structure

1CUR is a Single protein structure of sequence from Acidithiobacillus ferrooxidans. Full experimental information is available from OCA.

ReferenceReference

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

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-'''REDUCED RUSTICYANIN, NMR'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8947573}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8947573 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8947573}}
 ==About this Structure==
-CUR 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].
+CUR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUR OCA].
 ==Reference==
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 [[Category: Solution structure]]
 [[Category: Type 1 copper protein]]
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