Summary for 2X06
| Entry DOI | 10.2210/pdb2x06/pdb |
| Descriptor | L-SULFOLACTATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | oxidoreductase, hyperthermostable, coenzyme m, methanogens, coenzyme m biosynthesis, pro-s hydrogen transfer, nad-binding without a rossmann fold |
| Biological source | METHANOCALDOCOCCUS JANNASCHII |
| Total number of polymer chains | 8 |
| Total formula weight | 307958.87 |
| Authors | Irimia, A.,Madern, D.,Zaccai, G.,Vellieux, F.M.D. (deposition date: 2009-12-07, release date: 2009-12-15, Last modification date: 2024-11-13) |
| Primary citation | Irimia, A.,Madern, D.,Vellieux, F.M.D. Methanoarchaeal Sulfolactate Dehydrogenase: Prototype of a New Family of Nadh-Dependent Enzymes. Embo J., 23:1234-, 2004 Cited by PubMed Abstract: The crystal structure of the sulfolactate dehydrogenase from the hyperthermophilic and methanogenic archaeon Methanocaldococcus jannaschii was solved at 2.5 A resolution (PDB id. 1RFM). The asymmetric unit contains a tetramer of tight dimers. This structure, complexed with NADH, does not contain a cofactor-binding domain with 'Rossmann-fold' topology. Instead, the tertiary and quaternary structures indicate a novel fold. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers, which are therefore the smallest enzymatically active units. The protein was found to be a homodimer in solution by size-exclusion chromatography, analytical ultracentrifugation and small-angle neutron scattering. Various compounds were tested as putative substrates. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions. Based on sequence homology and phylogenetic analyses, several other enzymes were classified as belonging to this novel family of homologous (S)-2-hydroxyacid dehydrogenases. PubMed: 15014443DOI: 10.1038/SJ.EMBOJ.7600147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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