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| - | [[Image:1w9w.gif|left|200px]]<br /> | |
| - | <applet load="1w9w" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1w9w, resolution 2.10Å" /> | |
| - | '''STRUCTURE OF A BETA-1,3-GLUCAN BINDING CBM6 FROM BACILLUS HALODURANS IN COMPLEX WITH LAMINARIHEXAOSE'''<br /> | |
| | | | |
| - | ==Overview== | + | ==Structure of a beta-1,3-glucan binding CBM6 from Bacillus halodurans in complex with laminarihexaose== |
| - | Enzymes that hydrolyze insoluble complex polysaccharide structures contain, non-catalytic carbohydrate binding modules (CBMS) that play a pivotal role, in the action of these enzymes against recalcitrant substrates. Family 6, CBMs (CBM6s) are distinct from other CBM families in that these protein, modules contain multiple distinct ligand binding sites, a feature that, makes CBM6s particularly appropriate receptors for the beta-1,3-glucan, laminarin, which displays an extended U-shaped conformation. To, investigate the mechanism by which family 6 CBMs recognize laminarin, we, report the biochemical and structural properties of a CBM6 (designated, BhCBM6) that is located in an enzyme, which is shown, in this work, to, display beta-1,3-glucanase activity. BhCBM6 binds, beta-1,3-glucooligosaccharides with affinities of approximately 1 x 10(5), m(-1). The x-ray crystal structure of this CBM in complex with, laminarihexaose reveals similarity with the structures of other CBM6s but, a unique binding mode. The binding cleft in this protein is sealed at one, end, which prevents binding of linear polysaccharides such as cellulose, and the orientation of the sugar at this site prevents glycone extension, of the ligand and thus conferring specificity for the non-reducing ends of, glycans. The high affinity for extended beta-1,3-glucooligosaccharides is, conferred by interactions with the surface of the protein located between, the two binding sites common to CBM6s and thus reveals a third ligand, binding site in family 6 CBMs. This study therefore demonstrates how the, multiple binding clefts and highly unusual protein surface of family 6, CBMs confers the extensive range of specificities displayed by this, protein family. This is in sharp contrast to other families of CBMs where, variation in specificity between different members reflects differences in, the topology of a single binding site. | + | <StructureSection load='1w9w' size='340' side='right'caption='[[1w9w]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1w9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans Alkalihalobacillus halodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W9W 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]] 2.1Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1w9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w9w OCA], [https://pdbe.org/1w9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w9w RCSB], [https://www.ebi.ac.uk/pdbsum/1w9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w9w ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ENG1_HALH5 ENG1_HALH5] Cleaves internal linkages in 1,3-beta-glucan (PubMed:15501830, PubMed:28827308, PubMed:28781080). May contribute to plant biomass degradation (By similarity).[UniProtKB:Q47N06]<ref>PMID:15501830</ref> <ref>PMID:28781080</ref> <ref>PMID:28827308</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/w9/1w9w_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=1w9w ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Enzymes that hydrolyze insoluble complex polysaccharide structures contain non-catalytic carbohydrate binding modules (CBMS) that play a pivotal role in the action of these enzymes against recalcitrant substrates. Family 6 CBMs (CBM6s) are distinct from other CBM families in that these protein modules contain multiple distinct ligand binding sites, a feature that makes CBM6s particularly appropriate receptors for the beta-1,3-glucan laminarin, which displays an extended U-shaped conformation. To investigate the mechanism by which family 6 CBMs recognize laminarin, we report the biochemical and structural properties of a CBM6 (designated BhCBM6) that is located in an enzyme, which is shown, in this work, to display beta-1,3-glucanase activity. BhCBM6 binds beta-1,3-glucooligosaccharides with affinities of approximately 1 x 10(5) m(-1). The x-ray crystal structure of this CBM in complex with laminarihexaose reveals similarity with the structures of other CBM6s but a unique binding mode. The binding cleft in this protein is sealed at one end, which prevents binding of linear polysaccharides such as cellulose, and the orientation of the sugar at this site prevents glycone extension of the ligand and thus conferring specificity for the non-reducing ends of glycans. The high affinity for extended beta-1,3-glucooligosaccharides is conferred by interactions with the surface of the protein located between the two binding sites common to CBM6s and thus reveals a third ligand binding site in family 6 CBMs. This study therefore demonstrates how the multiple binding clefts and highly unusual protein surface of family 6 CBMs confers the extensive range of specificities displayed by this protein family. This is in sharp contrast to other families of CBMs where variation in specificity between different members reflects differences in the topology of a single binding site. |
| | | | |
| - | ==About this Structure==
| + | Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface.,van Bueren AL, Morland C, Gilbert HJ, Boraston AB J Biol Chem. 2005 Jan 7;280(1):530-7. Epub 2004 Oct 22. PMID:15501830<ref>PMID:15501830</ref> |
| - | 1W9W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W9W OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface., van Bueren AL, Morland C, Gilbert HJ, Boraston AB, J Biol Chem. 2005 Jan 7;280(1):530-7. Epub 2004 Oct 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15501830 15501830]
| + | </div> |
| - | [[Category: Bacillus halodurans]] | + | <div class="pdbe-citations 1w9w" style="background-color:#fffaf0;"></div> |
| - | [[Category: Single protein]] | + | == References == |
| - | [[Category: Boraston, A.B.]] | + | <references/> |
| - | [[Category: Bueren, A.L.Van.]] | + | __TOC__ |
| - | [[Category: NA]]
| + | </StructureSection> |
| - | [[Category: beta-glucan]]
| + | [[Category: Alkalihalobacillus halodurans]] |
| - | [[Category: carbohydrate binding]]
| + | [[Category: Large Structures]] |
| - | [[Category: carbohydrate-binding module]]
| + | [[Category: Boraston AB]] |
| - | [[Category: glycoside hydrolase]]
| + | [[Category: Van Bueren AL]] |
| - | [[Category: lectin]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:30:11 2007''
| + | |
| Structural highlights
Function
ENG1_HALH5 Cleaves internal linkages in 1,3-beta-glucan (PubMed:15501830, PubMed:28827308, PubMed:28781080). May contribute to plant biomass degradation (By similarity).[UniProtKB:Q47N06][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
Enzymes that hydrolyze insoluble complex polysaccharide structures contain non-catalytic carbohydrate binding modules (CBMS) that play a pivotal role in the action of these enzymes against recalcitrant substrates. Family 6 CBMs (CBM6s) are distinct from other CBM families in that these protein modules contain multiple distinct ligand binding sites, a feature that makes CBM6s particularly appropriate receptors for the beta-1,3-glucan laminarin, which displays an extended U-shaped conformation. To investigate the mechanism by which family 6 CBMs recognize laminarin, we report the biochemical and structural properties of a CBM6 (designated BhCBM6) that is located in an enzyme, which is shown, in this work, to display beta-1,3-glucanase activity. BhCBM6 binds beta-1,3-glucooligosaccharides with affinities of approximately 1 x 10(5) m(-1). The x-ray crystal structure of this CBM in complex with laminarihexaose reveals similarity with the structures of other CBM6s but a unique binding mode. The binding cleft in this protein is sealed at one end, which prevents binding of linear polysaccharides such as cellulose, and the orientation of the sugar at this site prevents glycone extension of the ligand and thus conferring specificity for the non-reducing ends of glycans. The high affinity for extended beta-1,3-glucooligosaccharides is conferred by interactions with the surface of the protein located between the two binding sites common to CBM6s and thus reveals a third ligand binding site in family 6 CBMs. This study therefore demonstrates how the multiple binding clefts and highly unusual protein surface of family 6 CBMs confers the extensive range of specificities displayed by this protein family. This is in sharp contrast to other families of CBMs where variation in specificity between different members reflects differences in the topology of a single binding site.
Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface.,van Bueren AL, Morland C, Gilbert HJ, Boraston AB J Biol Chem. 2005 Jan 7;280(1):530-7. Epub 2004 Oct 22. PMID:15501830[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Bueren AL, Morland C, Gilbert HJ, Boraston AB. Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface. J Biol Chem. 2005 Jan 7;280(1):530-7. Epub 2004 Oct 22. PMID:15501830 doi:10.1074/jbc.M410113200
- ↑ Pluvinage B, Fillo A, Massel P, Boraston AB. Structural Analysis of a Family 81 Glycoside Hydrolase Implicates Its Recognition of beta-1,3-Glucan Quaternary Structure. Structure. 2017 Sep 5;25(9):1348-1359.e3. doi: 10.1016/j.str.2017.06.019. Epub, 2017 Aug 3. PMID:28781080 doi:http://dx.doi.org/10.1016/j.str.2017.06.019
- ↑ Hettle A, Fillo A, Abe K, Massel P, Pluvinage B, Langelaan DN, Smith SP, Boraston AB. Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of beta-1,3-glucan. J Biol Chem. 2017 Oct 13;292(41):16955-16968. doi: 10.1074/jbc.M117.806711. Epub , 2017 Aug 21. PMID:28827308 doi:http://dx.doi.org/10.1074/jbc.M117.806711
- ↑ van Bueren AL, Morland C, Gilbert HJ, Boraston AB. Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface. J Biol Chem. 2005 Jan 7;280(1):530-7. Epub 2004 Oct 22. PMID:15501830 doi:10.1074/jbc.M410113200
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