ISDA: 1LUA

Deposition Date 2002-05-22

Release Date 2002-09-11

Last Version Date 2024-04-03

Entry Detail

PDB ID:

1LUA

Keywords:

OXIDOREDUCTASE

Title:

Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 complexed with NADP

Biological Source:

Source Organism(s):

Methylobacterium extorquens (Taxon ID: 272630)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.90 Å

R-Value Free:

0.22

R-Value Work:

0.18

R-Value Observed:

0.18

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Methylene Tetrahydromethanopt
Gene (Uniprot):mtdA
Chain IDs:A, B, C
Chain Length:287
Number of Molecules:3
Biological Source:Methylobacterium extorquens

UniProt ID:P55818 Pfam ID:PF09176

Ligand Molecules

NAP

Primary Citation

Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1.

Ermler, U, Hagemeier, C.H, Roth, A, Demmer, U, Grabarse, W, Warkentin, E, Vorholt, J.A, Vorholt, J.A, Chistoserdova, L, Lidstrom, M.E, Thauer, R.K.Show

Structure 10 1127 1137 (2002)

PMID: 12176390 DOI: 10.1016/S0969-2126(02)00802-X

Abstact

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.

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Primary Citation of related structures

Abstact

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