Structure of Methylene-Tetrahydromethanopterin Dehydrogenase from Methylobacterium extorquens AM1
| Autor: | Christoph H. Hagemeier, Eberhard Warkentin, Annette Roth, Ulrike Demmer, Julia A. Vorholt, Wolfgang Grabarse, Ulrich Ermler |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular crystal structure Protein Conformation Protein subunit Molecular Sequence Data Dehydrogenase Crystallography X-Ray Cofactor chemistry.chemical_compound conformational change Structural Biology Oxidoreductase Methylobacterium extorquens Humans Amino Acid Sequence Molecular Biology chemistry.chemical_classification Oxidoreductases Acting on CH-NH Group Donors tetrahydromethanopterin C1 metabolism Binding Sites Molecular Structure biology Tetrahydromethanopterin Active site biology.organism_classification tetrahydrofolate Protein Structure Tertiary Pterins Enzyme chemistry Biochemistry biology.protein Sequence Alignment NADP Protein Binding |
| Zdroj: | Structure. 10:1127-1137 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/s0969-2126(02)00802-x |
| Popis: | 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 α,β 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. |
| Databáze: | OpenAIRE |
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