1lkc

Crystal Structure of L-Threonine-O-3-Phosphate Decarboxylase from Salmonella entericaCrystal Structure of L-Threonine-O-3-Phosphate Decarboxylase from Salmonella enterica

Structural highlights

1lkc is a 1 chain structure with sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1kus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COBD_SALTY Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.^[1]

Evolutionary Conservation

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

References

↑ Brushaber KR, O'Toole GA, Escalante-Semerena JC. CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem. 1998 Jan 30;273(5):2684-91. PMID:9446573

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Brushaber KR, O'Toole GA, Escalante-Semerena JC. CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem. 1998 Jan 30;273(5):2684-91. PMID:9446573

[1]