1LU9: Structure Of Methylene-Tetrahydromethanopterin Dehydrogenase From Methylobacterium Extorquens Am1

NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 A resolution. The enzyme is present as a homotrimer. The alpha,beta fold of the monomer is related to that of methylene-H(4)F dehydrogenases, suggesting a common evolutionary origin. The position of the active site is located within a large crevice built up by the two domains of one subunit and one domain of a second subunit. Methylene-H(4)MPT could be modeled into the cleft, and crucial active site residues such as Phe18, Lys256, His260, and Thr102 were identified. The molecular basis of the different substrate specificities and different catalytic demands of MtdA compared to methylene-H(4)F dehydrogenases are discussed.
PDB ID: 1LU9Download
MMDB ID: 20671
PDB Deposition Date: 2002/5/22
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1LU9: trimeric; determined by author and by software (PISA)
Molecular Components in 1LU9
Label Count Molecule
Proteins (3 molecules)
Methylene Tetrahydromethanopterin Dehydrogenase
Molecule annotation
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