PDBsum entry 1soy

Unknown function

PDB id: 1soy

Contents

Protein chain

106 a.a. *

* Residue conservation analysis

PDB id:

1soy

Name:

Unknown function

Title:

Solution structure of the bacterial frataxin orthologue, cyay

Structure:

Cyay protein. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: cyay, b3807. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

M.Nair,S.Adinolfi,C.Pastore,G.Kelly,P.Temussi,A.Pastore

Key ref:

M.Nair et al. (2004). Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites. Structure, 12, 2037-2048. PubMed id: 15530368 DOI: 10.1016/j.str.2004.08.012

Date:

16-Mar-04 Release date: 23-Nov-04

Protein chain

P27838  (CYAY_ECOLI) -  Iron-sulfur cluster assembly protein CyaY from Escherichia coli (strain K12)

Seq: 106 a.a.

Struc: 106 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2004.08.012

Structure 12:2037-2048 (2004)

PubMed id: 15530368

Solution structure of the bacterial frataxin ortholog, CyaY: mapping the iron binding sites.

M.Nair, S.Adinolfi, C.Pastore, G.Kelly, P.Temussi, A.Pastore.

ABSTRACT

CyaY is the bacterial ortholog of frataxin, a small mitochondrial iron binding protein thought to be involved in iron sulphur cluster formation. Loss of frataxin function leads to the neurodegenerative disorder Friedreich's ataxia. We have solved the solution structure of CyaY and used the structural information to map iron binding onto the protein surface. Comparison of the behavior of wild-type CyaY with that of a mutant indicates that specific binding with a defined stoichiometry does not require aggregation and that the main binding site, which hosts both Fe(2+) and Fe(3+), occupies a highly anionic surface of the molecule. This function is conserved across species since the corresponding region of human frataxin is also able to bind iron, albeit with weaker affinity. The presence of secondary binding sites on CyaY, but not on frataxin, hints at a possible polymerization mechanism. We suggest mutations that may provide further insights into the frataxin function.

Selected figure(s)

Figure 1.
Figure 1. Solution Structure of CyaY and Comparison with the Crystal Structure and the Human Ortholog(A) A set of 20 energy-minimized conformers of bacterial frataxin CyaY superposed on the average structure (shown in red).(B) Average NMR structure showing the N- and C-terminal a helices packed against a six-stranded b sheet. The N and C termini are also indicated.(C) Pairwise superposition of the corresponding NMR (in green) and crystallographic (1ew4, in blue) structures of CyaY is shown.(D) Structural comparison of the NMR (1ly7, in green) and the crystal (1dlx, in green) structures of hfra(91-210) (in blue) using the same orientation as in (C).

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 2037-2048) copyright 2004.

Figure was selected by an automated process.