1nhc: Difference between revisions
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New page: left|200px<br /><applet load="1nhc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nhc, resolution 1.70Å" /> '''Structural insights ... |
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== | ==Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger== | ||
Endopolygalacturonase I is a processive enzyme, while the 60% sequence | <StructureSection load='1nhc' size='340' side='right'caption='[[1nhc]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nhc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NHC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=1nhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nhc OCA], [https://pdbe.org/1nhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nhc RCSB], [https://www.ebi.ac.uk/pdbsum/1nhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nhc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PGLR1_ASPNG PGLR1_ASPNG] Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nh/1nhc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nhc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred. | |||
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.,van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW FEBS Lett. 2003 Nov 20;554(3):462-6. PMID:14623112<ref>PMID:14623112</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nhc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspergillus niger]] | [[Category: Aspergillus niger]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Benen JA]] | |||
[[Category: Benen | [[Category: Dijkstra BW]] | ||
[[Category: Dijkstra | [[Category: Snijder HJ]] | ||
[[Category: Van Pouderoyen G]] | |||
[[Category: Snijder | |||
[[Category: | |||
Latest revision as of 12:39, 25 December 2024
Structural insights into the processivity of endopolygalacturonase I from Aspergillus nigerStructural insights into the processivity of endopolygalacturonase I from Aspergillus niger
Structural highlights
FunctionPGLR1_ASPNG Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEndopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger.,van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW FEBS Lett. 2003 Nov 20;554(3):462-6. PMID:14623112[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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