4PMH
The structure of rice weevil pectin methyl esterase
Summary for 4PMH
| Entry DOI | 10.2210/pdb4pmh/pdb |
| Descriptor | Pectinesterase (2 entities in total) |
| Functional Keywords | beta-barrel, pectin methyl esterase, hydrolase |
| Biological source | Sitophilus oryzae (Rice weevil) |
| Total number of polymer chains | 1 |
| Total formula weight | 39044.50 |
| Authors | Stenkamp, R.E.,Teller, D.C.,Behnke, C.A.,Reeck, G.R. (deposition date: 2014-05-21, release date: 2014-11-12, Last modification date: 2024-10-23) |
| Primary citation | Teller, D.C.,Behnke, C.A.,Pappan, K.,Shen, Z.,Reese, J.C.,Reeck, G.R.,Stenkamp, R.E. The structure of rice weevil pectin methylesterase. Acta Crystallogr.,Sect.F, 70:1480-1484, 2014 Cited by PubMed Abstract: Rice weevils (Sitophilus oryzae) use a pectin methylesterase (EC 3.1.1.11), along with other enzymes, to digest cell walls in cereal grains. The enzyme is a right-handed β-helix protein, but is circularly permuted relative to plant and bacterial pectin methylesterases, as shown by the crystal structure determination reported here. This is the first structure of an animal pectin methylesterase. Diffraction data were collected to 1.8 Å resolution some time ago for this crystal form, but structure solution required the use of molecular-replacement techniques that have been developed and similar structures that have been deposited in the last 15 years. Comparison of the structure of the rice weevil pectin methylesterase with that from Dickeya dandantii (formerly Erwinia chrysanthemi) indicates that the reaction mechanisms are the same for the insect, plant and bacterial pectin methylesterases. The similarity of the structure of the rice weevil enzyme to the Escherichia coli lipoprotein YbhC suggests that the evolutionary origin of the rice weevil enzyme was a bacterial lipoprotein, the gene for which was transferred to a primitive ancestor of modern weevils and other Curculionidae. Structural comparison of the rice weevil pectin methylesterase with plant and bacterial enzymes demonstrates that the rice weevil protein is circularly permuted relative to the plant and bacterial molecules. PubMed: 25372813DOI: 10.1107/S2053230X14020433 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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