4bhe | pdb_00004bhe
From Proteopedia
Methanococcus jannaschii serine hydroxymethyl-transferase in complex with PLP
Function
[GLYA_METJA] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.[1]
About this Structure
4bhe is a 12 chain structure. Full crystallographic information is available from OCA.
Reference
- ↑ Angelaccio S, Chiaraluce R, Consalvi V, Buchenau B, Giangiacomo L, Bossa F, Contestabile R. Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii. J Biol Chem. 2003 Oct 24;278(43):41789-97. Epub 2003 Aug 5. PMID:12902326 doi:https://dx.doi.org/10.1074/jbc.M306747200
