4GH5
Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)
Summary for 4GH5
| Entry DOI | 10.2210/pdb4gh5/pdb |
| Descriptor | Short-chain dehydrogenase/reductase SDR, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | rossmann fold, oxidoreductase |
| Biological source | Xanthobacter autotrophicus |
| Total number of polymer chains | 4 |
| Total formula weight | 111340.98 |
| Authors | Bakelar, J.W.,Johnson, S.J. (deposition date: 2012-08-07, release date: 2013-03-27, Last modification date: 2023-09-13) |
| Primary citation | Bakelar, J.W.,Sliwa, D.A.,Johnson, S.J. Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases. Arch.Biochem.Biophys., 533:62-68, 2013 Cited by PubMed Abstract: (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases (R- and S-HPCDH) are stereospecific enzymes that are central to the metabolism of propylene and epoxide in Xanthobacter autotrophicus. The bacterium produces R- and S-HPCDH simultaneously to facilitate transformation of R- and S-enantiomers of epoxypropane to a common achiral product 2-ketopropyl-CoM (2-KPC). Both R- and S-HPCDH are highly specific for their respective substrates as each enzyme displays less than 0.5% activity with the opposite substrate isomer. In order to elucidate the structural basis for stereospecificity displayed by R- and S-HPCDH we have determined substrate bound crystal structures of S-HPCDH to 1.6Å resolution. Comparisons to the previously reported product-bound structure of R-HPCDH reveal that although the placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. These structures demonstrate how chiral discrimination by R- and S-HPCDH results from alternative binding of the distal end of substrates within each substrate binding pocket. PubMed: 23474457DOI: 10.1016/j.abb.2013.02.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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