PDBsum entry 4jyf

Oxidoreductase

PDB id: 4jyf

Contents

Protein chain

347 a.a.

Ligands

SF4-SAH

1N7 ×5

H2S

CO3

Metals

_CL ×3

Waters ×382

PDB id:

4jyf

Name:

Oxidoreductase

Title:

X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound fe4s4 clusters.

Structure:

Fefe-hydrogenase maturase. Chain: a. Synonym: radical sam domain protein. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 243274. Strain: atcc 43589 / msb8 / dsm 3109 / jcm 10099. Gene: tm_1269, themadraft_0043. Expressed in: escherichia coli. Expression_system_taxid: 469008

Resolution:

1.45Å R-factor: 0.135 R-free: 0.166

Authors:

Y.Nicolet,R.Rohac,L.Martin,J.C.Fontecilla-Camps

Key ref:

Y.Nicolet et al. (2013). X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters. Proc Natl Acad Sci U S A, 110, 7188-7192. PubMed id: 23596207 DOI: 10.1073/pnas.1302388110

Date:

29-Mar-13 Release date: 01-May-13

Protein chain

Q9X0Z6  (HYDE_THEMA) -  [FeFe] hydrogenase maturase subunit HydE from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 348 a.a.

Struc: 347 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.8.-.-

DOI no: 10.1073/pnas.1302388110

Proc Natl Acad Sci U S A 110:7188-7192 (2013)

PubMed id: 23596207

X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters.

Y.Nicolet, R.Rohac, L.Martin, J.C.Fontecilla-Camps.

ABSTRACT

Fe4S4 clusters are very common versatile prosthetic groups in proteins. Their redox property of being sensitive to O2-induced oxidative damage is, for instance, used by the cell to sense oxygen levels and switch between aerobic and anaerobic metabolisms, as exemplified by the fumarate, nitrate reduction regulator (FNR). Using the hydrogenase maturase HydE from Thermotoga maritima as a template, we obtained several unusual forms of FeS clusters, some of which are associated with important structural changes. These structures represent intermediate states relevant to both FeS cluster assembly and degradation. We observe one Fe2S2 cluster bound by two cysteine persulfide residues. This observation lends structural support to a very recent Raman study, which reported that Fe4S4-to-Fe2S2 cluster conversion upon oxygen exposure in FNR resulted in concomitant production of cysteine persulfide as cluster ligands. Similar persulfide ligands have been observed in vitro for several other Fe4S4 cluster-containing proteins. We have also monitored FeS cluster conversion directly in our protein crystals. Our structures indicate that the Fe4S4-to-Fe2S2 change requires large structural modifications, which are most likely responsible for the dimer-monomer transition in FNR.