5c1e: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c1c|5c1c]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c1c|5c1c]]</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> | <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> | ||
<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=5c1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5c1e RCSB], [http://www.ebi.ac.uk/pdbsum/5c1e PDBsum]</span></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=5c1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1e OCA], [http://pdbe.org/5c1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c1e RCSB], [http://www.ebi.ac.uk/pdbsum/5c1e PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many pectin methylesterases (PMEs) are expressed in plants to modify plant cell-wall pectins for various physiological roles. These pectins are also attacked by PMEs from phytopathogens and phytophagous insects. The de-methylesterification by PMEs of the O6-methylester groups of the homogalacturonan (HG) component of pectin, exposing galacturonic acids, can occur processively or non-processively, respectively describing sequential versus single de-methylesterification events occurring before enzyme-substrate dissociation. The high-resolution X-ray structures of a PME from Aspergillus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10(2/3)-turn parallel beta helix (similar to but with less extensive loops than bacterial, plant and insect PMEs). Capillary electrophoresis shows that this PME is non-processive, halophilic and acidophilic. Molecular-dynamics simulations and electrostatic-potential calculations reveal very different behavior and properties compared to processive PMEs. Specifically, uncorrelated rotations are observed about the glycosidic bonds of a partially de-methylesterified decasaccharide model substrate, in sharp contrast to the correlated rotations of processive PMEs, and the substrate-binding groove is negatively not positively charged. | |||
Structure and Properties of Non-Processive, Salt-Requiring, Acidophilic Pectin Methylesterases from Aspergillus niger Provides Insights into the Key Determinants of Processivity Control.,Kent LM, Loo TS, Melton LD, Mercadante D, Williams MA, Jameson GB J Biol Chem. 2015 Nov 14. pii: jbc.M115.673152. PMID:26567911<ref>PMID:26567911</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5c1e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:02, 2 December 2015
Crystal Structure of the Pectin Methylesterase from Aspergillus niger in Penultimately Deglycosylated Form (N-acetylglucosamine Stub at Asn84)Crystal Structure of the Pectin Methylesterase from Aspergillus niger in Penultimately Deglycosylated Form (N-acetylglucosamine Stub at Asn84)
Structural highlights
Publication Abstract from PubMedMany pectin methylesterases (PMEs) are expressed in plants to modify plant cell-wall pectins for various physiological roles. These pectins are also attacked by PMEs from phytopathogens and phytophagous insects. The de-methylesterification by PMEs of the O6-methylester groups of the homogalacturonan (HG) component of pectin, exposing galacturonic acids, can occur processively or non-processively, respectively describing sequential versus single de-methylesterification events occurring before enzyme-substrate dissociation. The high-resolution X-ray structures of a PME from Aspergillus niger in deglycosylated and Asn-linked N-acetylglucosamine-stub forms reveal a 10(2/3)-turn parallel beta helix (similar to but with less extensive loops than bacterial, plant and insect PMEs). Capillary electrophoresis shows that this PME is non-processive, halophilic and acidophilic. Molecular-dynamics simulations and electrostatic-potential calculations reveal very different behavior and properties compared to processive PMEs. Specifically, uncorrelated rotations are observed about the glycosidic bonds of a partially de-methylesterified decasaccharide model substrate, in sharp contrast to the correlated rotations of processive PMEs, and the substrate-binding groove is negatively not positively charged. Structure and Properties of Non-Processive, Salt-Requiring, Acidophilic Pectin Methylesterases from Aspergillus niger Provides Insights into the Key Determinants of Processivity Control.,Kent LM, Loo TS, Melton LD, Mercadante D, Williams MA, Jameson GB J Biol Chem. 2015 Nov 14. pii: jbc.M115.673152. PMID:26567911[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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