Crystal Structure of Bacillus Subtilis YXEP Protein (APC1829), a Dinuclear Metal Binding Peptidase from M20 FamilyCrystal Structure of Bacillus Subtilis YXEP Protein (APC1829), a Dinuclear Metal Binding Peptidase from M20 Family

Structural highlights

1ysj is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

SCMP_BACSU Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine.[1]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Niehaus TD, Folz J, McCarty DR, Cooper AJL, Moraga Amador D, Fiehn O, Hanson AD. Identification of a metabolic disposal route for the oncometabolite S-(2-succino)cysteine in Bacillus subtilis. J Biol Chem. 2018 May 25;293(21):8255-8263. PMID:29626092 doi:10.1074/jbc.RA118.002925

1ysj, resolution 2.40Å

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