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2c0h

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X-ray structure of beta-mannanase from blue mussel Mytilus edulis

Structural highlights

2c0h is a 1 chain structure with sequence from Mytilus edulis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[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 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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xu B, Sellos D, Janson JC. Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) beta-mannanase gene. Eur J Biochem. 2002 Mar;269(6):1753-60. PMID:11895446
↑ Xu B, Hagglund P, Stalbrand H, Janson JC. endo-beta-1,4-Mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action. J Biotechnol. 2002 Jan 18;92(3):267-77. PMID:11689251
↑ Larsson AM, Anderson L, Xu B, Munoz IG, Uson I, Janson JC, Stalbrand H, Stahlberg J. Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis. J Mol Biol. 2006 Apr 14;357(5):1500-10. Epub 2006 Jan 31. PMID:16487541 doi:10.1016/j.jmb.2006.01.044
↑ Larsson AM, Anderson L, Xu B, Munoz IG, Uson I, Janson JC, Stalbrand H, Stahlberg J. Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis. J Mol Biol. 2006 Apr 14;357(5):1500-10. Epub 2006 Jan 31. PMID:16487541 doi:10.1016/j.jmb.2006.01.044

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c0h"

@@ Line 1: / Line 1: @@
-==X-RAY STRUCTURE OF BETA-MANNANASE FROM BLUE MUSSEL MYTILUS EDULIS==
-<StructureSection load='2c0h' size='340' side='right' caption='[[2c0h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+==X-ray structure of beta-mannanase from blue mussel Mytilus edulis==
+<StructureSection load='2c0h' size='340' side='right'caption='[[2c0h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c0h]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0H FirstGlance]. <br>
+<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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 1.6&#8491;</td></tr>
-<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0h RCSB], [http://www.ebi.ac.uk/pdbsum/2c0h PDBsum]</span></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>
+</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>
+    <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c0h" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Mannosidase|Mannosidase]]
+*[[Mannosidase 3D structures|Mannosidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Mannan endo-1,4-beta-mannosidase]]
+[[Category: Large Structures]]
 [[Category: Mytilus edulis]]
-[[Category: Anderson, L.]]
+[[Category: Anderson L]]
-[[Category: Janson, J C.]]
+[[Category: Janson J-C]]
-[[Category: Larsson, A M.]]
+[[Category: Larsson AM]]
-[[Category: Munoz, I G.]]
+[[Category: Munoz IG]]
-[[Category: Stahlberg, J.]]
+[[Category: Stahlberg J]]
-[[Category: Stalbrand, H.]]
+[[Category: Stalbrand H]]
-[[Category: Uson, I.]]
+[[Category: Uson I]]
-[[Category: Xu, B.]]
+[[Category: Xu B]]
-[[Category: Hydrolase]]
-[[Category: Mytilus eduli]]
-[[Category: Tim alpha/beta barrel]]

2c0h

From Proteopedia

Current revision

X-ray structure of beta-mannanase from blue mussel Mytilus edulis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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