5c1e: Difference between revisions
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==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)== | ||
<StructureSection load='5c1e' size='340' side='right' caption='[[5c1e]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5c1e' size='340' side='right'caption='[[5c1e]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c1e]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5c1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger_ATCC_1015 Aspergillus niger ATCC 1015]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C1E FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5c1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c1e OCA], [https://pdbe.org/5c1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c1e RCSB], [https://www.ebi.ac.uk/pdbsum/5c1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c1e ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G3YAL0_ASPNA G3YAL0_ASPNA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspergillus niger ATCC 1015]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Jameson | [[Category: Jameson GB]] | ||
[[Category: Kent | [[Category: Kent LM]] | ||
[[Category: Loo | [[Category: Loo TS]] | ||
[[Category: Melton | [[Category: Melton LD]] | ||
[[Category: Mercadante | [[Category: Mercadante D]] | ||
[[Category: Williams | [[Category: Williams MAK]] | ||
Revision as of 09:15, 7 June 2023
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
FunctionPublication 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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