1j9y: Difference between revisions
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==Crystal structure of mannanase 26A from Pseudomonas cellulosa== | ==Crystal structure of mannanase 26A from Pseudomonas cellulosa== | ||
<StructureSection load='1j9y' size='340' side='right' caption='[[1j9y]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1j9y' size='340' side='right'caption='[[1j9y]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9Y OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1j9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1J9Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Man26A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 "Cellvibrio cellulosa" Nagy et al. 2002])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Man26A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 "Cellvibrio cellulosa" Nagy et al. 2002])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1j9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9y OCA], [http://pdbe.org/1j9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j9y RCSB], [http://www.ebi.ac.uk/pdbsum/1j9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j9y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1j9y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1j9y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Mannosidase 3D structures|Mannosidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cellvibrio cellulosa nagy et al. 2002]] | [[Category: Cellvibrio cellulosa nagy et al. 2002]] | ||
[[Category: Large Structures]] | |||
[[Category: Mannan endo-1,4-beta-mannosidase]] | [[Category: Mannan endo-1,4-beta-mannosidase]] | ||
[[Category: Bolam, D N]] | [[Category: Bolam, D N]] | ||
Revision as of 10:28, 25 November 2020
Crystal structure of mannanase 26A from Pseudomonas cellulosaCrystal structure of mannanase 26A from Pseudomonas cellulosa
Structural highlights
Function[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.[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:11382747[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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