1WKV

Crystal structure of O-phosphoserine sulfhydrylase

Summary for 1WKV

• Entry DOI: 10.2210/pdb1wkv/pdb
• Descriptor: cysteine synthase, ACETATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: homodimer, open alpha/beta folding, transferase
• Biological source: Aeropyrum pernix
• Total number of polymer chains: 2
• Total formula weight: 84664.08

Authors

Oda, Y.,Mino, K.,Ishikawa, K.,Ataka, M. (deposition date: 2004-06-09, release date: 2005-06-28, Last modification date: 2011-07-13)

Primary citation

Oda, Y.,Mino, K.,Ishikawa, K.,Ataka, M.
Three-dimensional Structure of a New Enzyme, O-Phosphoserine Sulfhydrylase, involved in l-Cysteine Biosynthesis by a Hyperthermophilic Archaeon, Aeropyrum pernix K1, at 2.0A Resolution
J.Mol.Biol., 351:334-344, 2005

PubMed Abstract: O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determined at 2.0A resolution using the method of multi-wavelength anomalous dispersion. A monomer consists of three domains, including an N-terminal domain with a new alpha/beta fold. The topology folds of the middle and C-terminal domains were similar to those of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the cystathionine beta-synthase from human. The cofactor, pyridoxal 5'-phosphate, is bound in a cleft between the middle and C-terminal domains through a covalent linkage to Lys127. Based on the structure determined, O-phospho-l-serine could be rationally modeled into the active site of the enzyme. An enzyme-substrate complex model and a mutation experiment revealed that Arg297, unique to hyperthermophilic archaea, is one of the most crucial residues for O-phosphoserine sulfhydrylation activity. There are more hydrophobic areas and less electric charges at the dimer interface, compared to the S.typhimurium O-acetylserine sulfhydrylase.

PubMed: 16005886
DOI: 10.1016/j.jmb.2005.05.064

Experimental method

X-RAY DIFFRACTION (2 Å)