8TMS
Crystal structure of bacterial pectin methylesterase PmeC2 from rumen Butyrivibrio
Summary for 8TMS
Entry DOI | 10.2210/pdb8tms/pdb |
Descriptor | Pectinesterase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | pectin methylesterase, butyrivibrio, rumen, pectin, methanol, methane, sugar binding protein |
Biological source | Butyrivibrio fibrisolvens |
Total number of polymer chains | 4 |
Total formula weight | 138800.98 |
Authors | Carbone, V.,Reilly, K.,Sang, C.,Schofield, L.,Ronimus, R.,Kelly, W.J.,Attwood, G.T.,Palevich, N. (deposition date: 2023-07-30, release date: 2023-08-16, Last modification date: 2023-10-11) |
Primary citation | Carbone, V.,Reilly, K.,Sang, C.,Schofield, L.R.,Ronimus, R.S.,Kelly, W.J.,Attwood, G.T.,Palevich, N. Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen Butyrivibrio . Int J Mol Sci, 24:-, 2023 Cited by PubMed Abstract: Pectin is a complex polysaccharide that forms a substantial proportion of the plant's middle lamella of forage ingested by grazing ruminants. Methanol in the rumen is derived mainly from methoxy groups released from pectin by the action of pectin methylesterase (PME) and is subsequently used by rumen methylotrophic methanogens that reduce methanol to produce methane (CH). Members of the genus are key pectin-degrading rumen bacteria that contribute to methanol formation and have important roles in fibre breakdown, protein digestion, and the biohydrogenation of fatty acids. Therefore, methanol release from pectin degradation in the rumen is a potential target for CH mitigation technologies. Here, we present the crystal structures of PMEs belonging to the carbohydrate esterase family 8 (CE8) from and , determined to a resolution of 2.30 Å. These enzymes, like other PMEs, are right-handed β-helical proteins with a well-defined catalytic site and reaction mechanisms previously defined in insect, plant, and other bacterial pectin methylesterases. Potential substrate binding domains are also defined for the enzymes. PubMed: 37762041DOI: 10.3390/ijms241813738 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report