2c0h: Difference between revisions
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== | ==X-ray structure of beta-mannanase from blue mussel Mytilus edulis== | ||
Endo-beta-1,4-d-mannanase is the key depolymerizing enzyme for | <StructureSection load='2c0h' size='340' side='right'caption='[[2c0h]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2c0h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0H 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]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2c0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0h OCA], [https://pdbe.org/2c0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0h RCSB], [https://www.ebi.ac.uk/pdbsum/2c0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MANA_MYTED MANA_MYTED] Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 preferentially to M3, and less preferentially to mannose (M1), plus very little M2. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose.<ref>PMID:11895446</ref> <ref>PMID:11689251</ref> <ref>PMID:16487541</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/c0/2c0h_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2c0h ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endo-beta-1,4-d-mannanase is the key depolymerizing enzyme for beta-1,4-mannan polymers present in the cell walls of plants and some algae, as well as in some types of plant seeds. Endo-1,4-beta-mannanase from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined to 1.6A resolution using the multiple-wavelength anomalous dispersion method at the selenium K edge with selenomethionyl MeMan5A expressed in the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure showed a (betaalpha)(8)-barrel fold. An unusually large number of histidine side-chains are exposed on the surface, which may relate to its location within the crystalline style of the digestive tract of the mussel. Kinetic analysis of MeMan5A revealed that the enzyme requires at least six subsites for efficient hydrolysis. Mannotetraose (M4) and mannopentaose (M5) were shown to interact with subsites -3 to +1, and -3 to +2, respectively. A clear kinetic threshold was observed when going from M4 to M5, indicating that the +2 subsite provides important interaction in the hydrolysis of short oligomeric mannose substrates. The catalytic centre motif at subsite -1 found in superfamily GH clan A is, as expected, conserved in MeMan5A, but the architecture of the catalytic cleft differs significantly from other GH 5 enzyme structures. We therefore suggest that MeMan5A represents a new subfamily in GH 5. | |||
Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis.,Larsson AM, Anderson L, Xu B, Munoz IG, Uson I, Janson JC, Stalbrand H, Stahlberg J J Mol Biol. 2006 Apr 14;357(5):1500-10. Epub 2006 Jan 31. PMID:16487541<ref>PMID:16487541</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2c0h" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Mannosidase 3D structures|Mannosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mytilus edulis]] | [[Category: Mytilus edulis]] | ||
[[Category: Anderson L]] | |||
[[Category: Anderson | [[Category: Janson J-C]] | ||
[[Category: Janson | [[Category: Larsson AM]] | ||
[[Category: Larsson | [[Category: Munoz IG]] | ||
[[Category: Munoz | [[Category: Stahlberg J]] | ||
[[Category: Stahlberg | [[Category: Stalbrand H]] | ||
[[Category: Stalbrand | [[Category: Uson I]] | ||
[[Category: Uson | [[Category: Xu B]] | ||
[[Category: Xu | |||
Latest revision as of 12:20, 9 May 2024
X-ray structure of beta-mannanase from blue mussel Mytilus edulisX-ray structure of beta-mannanase from blue mussel Mytilus edulis
Structural highlights
FunctionMANA_MYTED Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 preferentially to M3, and less preferentially to mannose (M1), plus very little M2. Does not hydrolyze mannobiose or mannotriose. Does not hydrolyze xlyan, starch, cellulose or galactose.[1] [2] [3] 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 PubMedEndo-beta-1,4-d-mannanase is the key depolymerizing enzyme for beta-1,4-mannan polymers present in the cell walls of plants and some algae, as well as in some types of plant seeds. Endo-1,4-beta-mannanase from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined to 1.6A resolution using the multiple-wavelength anomalous dispersion method at the selenium K edge with selenomethionyl MeMan5A expressed in the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure showed a (betaalpha)(8)-barrel fold. An unusually large number of histidine side-chains are exposed on the surface, which may relate to its location within the crystalline style of the digestive tract of the mussel. Kinetic analysis of MeMan5A revealed that the enzyme requires at least six subsites for efficient hydrolysis. Mannotetraose (M4) and mannopentaose (M5) were shown to interact with subsites -3 to +1, and -3 to +2, respectively. A clear kinetic threshold was observed when going from M4 to M5, indicating that the +2 subsite provides important interaction in the hydrolysis of short oligomeric mannose substrates. The catalytic centre motif at subsite -1 found in superfamily GH clan A is, as expected, conserved in MeMan5A, but the architecture of the catalytic cleft differs significantly from other GH 5 enzyme structures. We therefore suggest that MeMan5A represents a new subfamily in GH 5. Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis.,Larsson AM, Anderson L, Xu B, Munoz IG, Uson I, Janson JC, Stalbrand H, Stahlberg J J Mol Biol. 2006 Apr 14;357(5):1500-10. Epub 2006 Jan 31. PMID:16487541[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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