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8TMS

Crystal structure of bacterial pectin methylesterase PmeC2 from rumen Butyrivibrio

Summary for 8TMS
Entry DOI10.2210/pdb8tms/pdb
DescriptorPectinesterase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordspectin methylesterase, butyrivibrio, rumen, pectin, methanol, methane, sugar binding protein
Biological sourceButyrivibrio fibrisolvens
Total number of polymer chains4
Total formula weight138800.98
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 citationCarbone, 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: 37762041
DOI: 10.3390/ijms241813738
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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數據於2024-11-06公開中

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