PDBsum entry 1n9c

Electron transport

PDB id: 1n9c

Contents

Protein chain

71 a.a. *

Ligands

HEC

* Residue conservation analysis

PDB id:

1n9c

Name:

Electron transport

Title:

Structure and dynamics of reduced bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes

Structure:

CytochromE C-553. Chain: a. Fragment: soluble part of membrane-anchored cytochromE C. Synonym: c553. Engineered: yes

Source:

Sporosarcina pasteurii. Organism_taxid: 1474. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

I.Bartalesi,I.Bertini,A.Rosato

Key ref:

I.Bartalesi et al. (2003). Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes. Biochemistry, 42, 739-745. PubMed id: 12534286 DOI: 10.1021/bi0266028

Date:

23-Nov-02 Release date: 04-Feb-03

Protein chain

P82599  (CY553_SPOPA) -  Cytochrome c-553 from Sporosarcina pasteurii

Seq: 92 a.a.

Struc: 71 a.a.

DOI no: 10.1021/bi0266028

Biochemistry 42:739-745 (2003)

PubMed id: 12534286

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes.

I.Bartalesi, I.Bertini, A.Rosato.

ABSTRACT

The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.