Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i>
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 rume...
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MDPI AG
2023-09-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/18/13738 |
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| author | Vincenzo Carbone Kerri Reilly Carrie Sang Linley R. Schofield Ron S. Ronimus William J. Kelly Graeme T. Attwood Nikola Palevich |
| author_facet | Vincenzo Carbone Kerri Reilly Carrie Sang Linley R. Schofield Ron S. Ronimus William J. Kelly Graeme T. Attwood Nikola Palevich |
| author_sort | Vincenzo Carbone |
| collection | DOAJ |
| description | 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<sub>4</sub>). Members of the genus <i>Butyrivibrio</i> 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<sub>4</sub> mitigation technologies. Here, we present the crystal structures of PMEs belonging to the carbohydrate esterase family 8 (CE8) from <i>Butyrivibrio proteoclasticus</i> and <i>Butyrivibrio fibrisolvens</i>, 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. |
| first_indexed | 2024-03-10T22:41:12Z |
| format | Article |
| id | doaj.art-647b0ff60c0243148b4a83da3b133bb6 |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T22:41:12Z |
| publishDate | 2023-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-647b0ff60c0243148b4a83da3b133bb62023-11-19T11:02:24ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-09-0124181373810.3390/ijms241813738Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i>Vincenzo Carbone0Kerri Reilly1Carrie Sang2Linley R. Schofield3Ron S. Ronimus4William J. Kelly5Graeme T. Attwood6Nikola Palevich7AgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandAgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New ZealandPectin 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<sub>4</sub>). Members of the genus <i>Butyrivibrio</i> 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<sub>4</sub> mitigation technologies. Here, we present the crystal structures of PMEs belonging to the carbohydrate esterase family 8 (CE8) from <i>Butyrivibrio proteoclasticus</i> and <i>Butyrivibrio fibrisolvens</i>, 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.https://www.mdpi.com/1422-0067/24/18/13738pectin methylesterase<i>Butyrivibrio</i>rumenpectinmethanolmethane |
| spellingShingle | Vincenzo Carbone Kerri Reilly Carrie Sang Linley R. Schofield Ron S. Ronimus William J. Kelly Graeme T. Attwood Nikola Palevich Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> International Journal of Molecular Sciences pectin methylesterase <i>Butyrivibrio</i> rumen pectin methanol methane |
| title | Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> |
| title_full | Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> |
| title_fullStr | Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> |
| title_full_unstemmed | Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> |
| title_short | Crystal Structures of Bacterial Pectin Methylesterases Pme8A and PmeC2 from Rumen <i>Butyrivibrio</i> |
| title_sort | crystal structures of bacterial pectin methylesterases pme8a and pmec2 from rumen i butyrivibrio i |
| topic | pectin methylesterase <i>Butyrivibrio</i> rumen pectin methanol methane |
| url | https://www.mdpi.com/1422-0067/24/18/13738 |
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