PDBsum entry 4lw2

Lyase

PDB id: 4lw2

Contents

Protein chains

399 a.a.

Ligands

PLP ×3

GOL ×3

Waters ×1107

PDB id:

4lw2

Name:

Lyase

Title:

Structural changes during cysteine desulfurase csda and sulfur- acceptor csde interactions provide insight into the trans- persulfuration

Structure:

Cysteine sulfinate desulfinase. Chain: a, b, c. Synonym: csd. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b2810, csda, jw2781, ygdj. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.80Å R-factor: 0.167 R-free: 0.212

Authors:

S.Kim,S.Y.Park

Key ref:

S.Kim and S.Park (2013). Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration. J Biol Chem, 288, 27172-27180. PubMed id: 23913692 DOI: 10.1074/jbc.M113.480277

Date:

26-Jul-13 Release date: 07-Aug-13

Protein chains

Q46925  (CSDA_ECOLI) -  Cysteine desulfurase CsdA from Escherichia coli (strain K12)

Seq: 401 a.a.

Struc: 399 a.a.

Enzyme reactions

• Enzyme class 1: E.C.2.8.1.7 - cysteine desulfurase.
• Reaction: (sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine

(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine (Bound ligand (Het Group name = GOL) matches with 50.00% similarity)

• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PLP) matches with 93.75% similarity)

• Enzyme class 2: E.C.4.4.1.16 - selenocysteine lyase.
• Reaction: L-selenocysteine + AH2 = hydrogenselenide + L-alanine + A + H⁺

L-selenocysteine + AH2 = hydrogenselenide + L-alanine + + H(+) (Bound ligand (Het Group name = GOL) matches with 50.00% similarity)

• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PLP) matches with 93.75% similarity)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1074/jbc.M113.480277

J Biol Chem 288:27172-27180 (2013)

PubMed id: 23913692

Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration.

S.Kim, S.Park.

ABSTRACT

In Escherichia coli, three cysteine desulfurases (IscS, SufS, and CsdA) initiate the delivery of sulfur for various biological processes such as the biogenesis of Fe-S clusters. The sulfur generated as persulfide on a cysteine residue of cysteine desulfurases is further transferred to Fe-S scaffolds (e.g. IscU) or to intermediate cysteine-containing sulfur acceptors (e.g. TusA, SufE, and CsdE) prior to its utilization. Here, we report the structures of CsdA and the CsdA-CsdE complex, which provide insight into the sulfur transfer mediated by the trans-persulfuration reaction. Analysis of the structures indicates that the conformational flexibility of the active cysteine loop in CsdE is essential for accepting the persulfide from the cysteine of CsdA. Additionally, CsdA and CsdE invoke a different binding mode than those of previously reported cysteine desulfurase (IscS) and sulfur acceptors (TusA and IscU). Moreover, the conservation of interaction-mediating residues between CsdA/SufS and CsdE/SufE further suggests that the SufS-SufE interface likely resembles that of CsdA and CsdE.