This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1cur

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cur.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cur.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cur| PDB=1cur | SCENE= }}
{{STRUCTURE_1cur| PDB=1cur | SCENE= }}
-
'''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==
==About this Structure==
-
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].
+
1CUR 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==
==Reference==
Line 28: Line 32:
[[Category: Solution structure]]
[[Category: Solution structure]]
[[Category: Type 1 copper protein]]
[[Category: Type 1 copper protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:07:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:24:01 2008''

Revision as of 18:24, 30 June 2008

Image:1cur.png

Template:STRUCTURE 1cur

REDUCED RUSTICYANIN, NMR

Template:ABSTRACT PUBMED 8947573

About this Structure

1CUR is a Single protein structure of sequence from Acidithiobacillus ferrooxidans. Full experimental 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 Mon Jun 30 21:24:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cur"
Personal tools