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== | ==Substrate distortion by beta-mannanase from Pseudomonas cellulosa== | ||
<StructureSection load='1gw1' size='340' side='right'caption='[[1gw1]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gw1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GW1 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]] 1.65Å</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=MAF:2-DEOXY-2-FLUORO-ALPHA-D-MANNOSE'>MAF</scene>, <scene name='pdbligand=MBF:2-DEOXY-2-FLUORO-BETA-D-MANNOSE'>MBF</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NIN:DINITROPHENYLENE'>NIN</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1gw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gw1 OCA], [https://pdbe.org/1gw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gw1 RCSB], [https://www.ebi.ac.uk/pdbsum/1gw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gw1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MANA_CELJU MANA_CELJU] Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.<ref>PMID:7848261</ref> <ref>PMID:11064195</ref> | |||
== 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/gw/1gw1_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=1gw1 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of Pseudomonas cellulosa mannanase 26A has been solved by multiple isomorphous replacement and refined at 1.85 A resolution to an R-factor of 0.182 (R-free = 0.211). The enzyme comprises (beta/alpha)(8)-barrel architecture with two catalytic glutamates at the ends of beta-strands 4 and 7 in precisely the same location as the corresponding glutamates in other 4/7-superfamily glycoside hydrolase enzymes (clan GH-A glycoside hydrolases). The family 26 glycoside hydrolases are therefore members of clan GH-A. Functional analyses of mannanase 26A, informed by the crystal structure of the enzyme, provided important insights into the role of residues close to the catalytic glutamates. These data showed that Trp-360 played a critical role in binding substrate at the -1 subsite, whereas Tyr-285 was important to the function of the nucleophile catalyst. His-211 in mannanase 26A does not have the same function as the equivalent asparagine in the other GH-A enzymes. The data also suggest that Trp-217 and Trp-162 are important for the activity of mannanase 26A against mannooligosaccharides but are less important for activity against polysaccharides. | |||
Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding.,Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:011382747<ref>PMID:011382747</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gw1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Mannosidase 3D structures|Mannosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cellvibrio japonicus]] | [[Category: Cellvibrio japonicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Davies GJ]] | |||
[[Category: Davies | [[Category: Ducros V]] | ||
[[Category: Ducros | [[Category: Gilbert HJ]] | ||
[[Category: Gilbert | [[Category: Szabo L]] | ||
[[Category: Szabo | [[Category: Withers SG]] | ||
[[Category: Withers | [[Category: Zechel DL]] | ||
[[Category: Zechel | |||
Latest revision as of 11:28, 6 November 2024
Substrate distortion by beta-mannanase from Pseudomonas cellulosaSubstrate distortion by beta-mannanase from Pseudomonas cellulosa
Structural highlights
FunctionMANA_CELJU Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan. Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides.[1] [2] 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 PubMedThe crystal structure of Pseudomonas cellulosa mannanase 26A has been solved by multiple isomorphous replacement and refined at 1.85 A resolution to an R-factor of 0.182 (R-free = 0.211). The enzyme comprises (beta/alpha)(8)-barrel architecture with two catalytic glutamates at the ends of beta-strands 4 and 7 in precisely the same location as the corresponding glutamates in other 4/7-superfamily glycoside hydrolase enzymes (clan GH-A glycoside hydrolases). The family 26 glycoside hydrolases are therefore members of clan GH-A. Functional analyses of mannanase 26A, informed by the crystal structure of the enzyme, provided important insights into the role of residues close to the catalytic glutamates. These data showed that Trp-360 played a critical role in binding substrate at the -1 subsite, whereas Tyr-285 was important to the function of the nucleophile catalyst. His-211 in mannanase 26A does not have the same function as the equivalent asparagine in the other GH-A enzymes. The data also suggest that Trp-217 and Trp-162 are important for the activity of mannanase 26A against mannooligosaccharides but are less important for activity against polysaccharides. Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding.,Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:011382747[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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