9MM2
Crystal structure of bacterial pectin methylesterase PmeC5 from B. fibrisolvens D1T
Summary for 9MM2
| Entry DOI | 10.2210/pdb9mm2/pdb |
| Descriptor | Putative cell wall binding repeat-containing protein, MAGNESIUM ION, SODIUM ION, ... (6 entities in total) |
| Functional Keywords | pectin methylesterase, sugar binding protein |
| Biological source | Butyrivibrio fibrisolvens DSM 3071 |
| Total number of polymer chains | 1 |
| Total formula weight | 50094.35 |
| Authors | Carbone, V.,Reilly, K.,Sang, C.,Schofield, L.,Ronimus, R.,Attwood, G.T.,Palevich, N. (deposition date: 2024-12-19, release date: 2025-01-15, Last modification date: 2025-06-18) |
| Primary citation | Carbone, V.,Reilly, K.,Sang, C.,Schofield, L.R.,Kelly, W.J.,Ronimus, R.S.,Attwood, G.T.,Palevich, N. Crystal Structure of the Multidomain Pectin Methylesterase PmeC5 from Butyrivibrio fibrisolvens D1 T. Biomolecules, 15:-, 2025 Cited by PubMed Abstract: Pectin is a dynamic and complex polysaccharide that forms a substantial proportion of the primary plant cell wall and middle lamella of forage ingested by grazing ruminants. Pectin methylesterases (PMEs) are enzymes that belongs to the carbohydrate esterase family 8 (CE8) and catalyze the demethylesterification of pectin, a key polysaccharide in cell walls. Here we present the crystal structure of the catalytic domain of PmeC5 that is associated with a gene from D1 that encodes a large secreted pectinesterase family protein (2089 aa) determined to a resolution of 1.33 Å. Protein in silico modelling of the secreted pectinesterase confirmed the presence of an additional pectate lyase (PL9) and adhesin-like domains. The structure of PmeC5 was the characteristic right-handed parallel β-helical topology and active site residues of Asp231, Asp253, and Arg326 typical of the enzyme class. PmeC5 is a large modular enzyme that is characteristic of rumen megaplasmids and plays a central role in degrading plant cell wall components and releasing methanol in the rumen environment. Such secreted PMEs are significant contributors to plant fiber digestion and methane production, making them attractive targets for both methane mitigation strategies and livestock productivity enhancement. PubMed: 40427613DOI: 10.3390/biom15050720 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.33 Å) |
Structure validation
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