3njv

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(New page: '''Unreleased structure''' The entry 3njv is ON HOLD Authors: Jensen, M.H., Otten, H., Christensen, U., Borchert, T.V., Christensen, L.L.H., Larsen, S., Lo Leggio, L. Description: Rham...)
Current revision (08:04, 9 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3njv is ON HOLD
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==Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex==
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<StructureSection load='3njv' size='340' side='right'caption='[[3njv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3njv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GTR:BETA-D-GALACTOPYRANURONIC+ACID'>GTR</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3njv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njv OCA], [https://pdbe.org/3njv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3njv RCSB], [https://www.ebi.ac.uk/pdbsum/3njv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3njv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RGLA_ASPAC RGLA_ASPAC] Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.<ref>PMID:20851126</ref> <ref>PMID:8587995</ref> <ref>PMID:9576783</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nj/3njv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3njv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We present here the first experimental evidence for bound substrate in the active site of a rhamnogalacturonan lyase belonging to family 4 of polysaccharide lyases, Aspergillus aculeatus rhamnogalacturonan lyase (RGL4). RGL4 is involved in the degradation of rhamnogalacturonan-I, an important pectic plant cell wall polysaccharide. Based on the previously determined wild-type structure, enzyme variants RGL4_H210A and RGL4_K150A have been produced and characterized both kinetically and structurally, showing that His210 and Lys150 are key active-site residues. Crystals of the RGL4_K150A variant soaked with a rhamnogalacturonan digest gave a clear picture of substrate bound in the -3/+3 subsites. The crystallographic and kinetic studies on RGL4, and structural and sequence comparison to other enzymes in the same and other PL families, enable us to propose a detailed reaction mechanism for the beta-elimination on [-,2)-alpha-l-rhamno-(1,4)-alpha-d-galacturonic acid-(1,-]. The mechanism differs significantly from the one established for pectate lyases, in which most often calcium ions are engaged in catalysis.
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Authors: Jensen, M.H., Otten, H., Christensen, U., Borchert, T.V., Christensen, L.L.H., Larsen, S., Lo Leggio, L.
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Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus.,Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL J Mol Biol. 2010 Sep 17. PMID:20851126<ref>PMID:20851126</ref>
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Description: Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 30 13:36:13 2010''
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<div class="pdbe-citations 3njv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aspergillus aculeatus]]
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[[Category: Large Structures]]
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[[Category: Borchert TV]]
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[[Category: Christensen LLH]]
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[[Category: Christensen U]]
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[[Category: Jensen MH]]
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[[Category: Larsen S]]
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[[Category: Lo Leggio L]]
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[[Category: Otten H]]

Current revision

Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex

PDB ID 3njv

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