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| | ==The structure of rice weevil pectin methyl esterase== | | ==The structure of rice weevil pectin methyl esterase== |
| - | <StructureSection load='4pmh' size='340' side='right' caption='[[4pmh]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='4pmh' size='340' side='right'caption='[[4pmh]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pmh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PMH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sitophilus_oryzae Sitophilus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PMH FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.11 3.1.1.11] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pmh RCSB], [http://www.ebi.ac.uk/pdbsum/4pmh PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pmh OCA], [https://pdbe.org/4pmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pmh RCSB], [https://www.ebi.ac.uk/pdbsum/4pmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pmh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PME_SITOR PME_SITOR] Pectinesterase which probably plays an important role in the digestion of plant cell walls.<ref>PMID:16341253</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4pmh" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Behnke, C A]] | + | [[Category: Sitophilus oryzae]] |
| - | [[Category: Reeck, G R]] | + | [[Category: Behnke CA]] |
| - | [[Category: Stenkamp, R E]] | + | [[Category: Reeck GR]] |
| - | [[Category: Teller, D C]] | + | [[Category: Stenkamp RE]] |
| - | [[Category: Beta-barrel]] | + | [[Category: Teller DC]] |
| - | [[Category: Pectin methyl esterase]]
| + | |
| Structural highlights
Function
PME_SITOR Pectinesterase which probably plays an important role in the digestion of plant cell walls.[1]
Publication Abstract from PubMed
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 beta-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 A 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.
The structure of rice weevil pectin methylesterase.,Teller DC, Behnke CA, Pappan K, Shen Z, Reese JC, Reeck GR, Stenkamp RE Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1480-4. doi:, 10.1107/S2053230X14020433. Epub 2014 Oct 25. PMID:25372813[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shen Z, Pappan K, Mutti NS, He QJ, Denton M, Zhang Y, Kanost MR, Reese JC, Reeck GR. Pectinmethylesterase from the rice weevil, Sitophilus oryzae: cDNA isolation and sequencing, genetic origin, and expression of the recombinant enzyme. J Insect Sci. 2005;5:21. PMID:16341253 doi:10.1093/jis/5.1.21
- ↑ Teller DC, Behnke CA, Pappan K, Shen Z, Reese JC, Reeck GR, Stenkamp RE. The structure of rice weevil pectin methylesterase. Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1480-4. doi:, 10.1107/S2053230X14020433. Epub 2014 Oct 25. PMID:25372813 doi:http://dx.doi.org/10.1107/S2053230X14020433
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