4lw4

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

Structural highlights

4lw4 is a 4 chain structure with sequence from Escherichia coli IHE3034 and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.01Å
Ligands:PLP
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CSDA_ECOLI Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. L-cysteine sulfinic acid is the best substrate. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.[1]

Publication Abstract from PubMed

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 are 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. Herein, we report structures of CsdA, and 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.

Structural changes during cysteine desulfurase CsdA and sulfur-acceptor CsdE interactions provide insight into the trans-persulfuration.,Kim S, Park S J Biol Chem. 2013 Aug 2. PMID:23913692[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000 Aug 4;275(31):23769-73. PMID:10829016 doi:10.1074/jbc.M000926200
  2. Kim S, Park S. Structural changes during cysteine desulfurase CsdA and sulfur-acceptor CsdE interactions provide insight into the trans-persulfuration. J Biol Chem. 2013 Aug 2. PMID:23913692 doi:10.1074/jbc.M113.480277

Contents


PDB ID 4lw4

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