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5t7a

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Current revision (14:19, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5t7a' size='340' side='right'caption='[[5t7a]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5t7a' size='340' side='right'caption='[[5t7a]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t7a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bachd Bachd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T7A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T7A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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</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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BH0236 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272558 BACHD])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7a OCA], [http://pdbe.org/5t7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t7a RCSB], [http://www.ebi.ac.uk/pdbsum/5t7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7a ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t7a OCA], [https://pdbe.org/5t7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t7a RCSB], [https://www.ebi.ac.uk/pdbsum/5t7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t7a ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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>
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BH0236 from Bacillus halodurans is a multimodular beta-1,3-glucanase comprising an N-terminal family 81 glycoside hydrolase catalytic module, an internal family 6 carbohydrate-binding module (CBM) that binds the nonreducing end of beta-1,3-glucan chains, and an uncharacterized C-terminal module classified into CBM family 56. Here, we determined that this latter CBM, BhCBM56, bound the soluble beta-1,3-glucan laminarin with a dissociation constant (Kd ) of approximately 26 mum and displayed higher affinity for insoluble beta-1,3-glucans with Kd values of approximately 2-10 mum but lacked affinity for beta-1,3-glucooligosaccharides. The X-ray crystal structure of BhCBM56 and NMR-derived chemical shift mapping of the binding site revealed a beta-sandwich fold, with the face of one beta-sheet possessing the beta-1,3-glucan-binding surface. On the basis of the functional and structural properties of BhCBM56, we propose that it binds a quaternary polysaccharide structure, most likely the triple helix adopted by polymerized beta-1,3-glucans. Consistent with the BhCBM56 and BhCBM6/56 binding profiles, deletion of the CBM56 from BH0236 decreased activity of the enzyme on the insoluble beta-1,3-glucan curdlan but not on soluble laminarin; additional deletion of the CBM6 also did not affect laminarin degradation but further decreased curdlan hydrolysis. The pseudo-atomic solution structure of BH0236 determined by small-angle X-ray scattering revealed structural insights into the nature of avid binding by the BhCBM6/56 pair and how the orientation of the active site in the catalytic module factors into recognition and degradation of beta-1,3-glucans. Our findings reinforce the notion that catalytic modules and their cognate CBMs have complementary specificities, including targeting of polysaccharide quaternary structure.
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Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of beta-1,3-glucan.,Hettle A, Fillo A, Abe K, Massel P, Pluvinage B, Langelaan DN, Smith SP, Boraston AB J Biol Chem. 2017 Oct 13;292(41):16955-16968. doi: 10.1074/jbc.M117.806711. Epub , 2017 Aug 21. PMID:28827308<ref>PMID:28827308</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5t7a" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bachd]]
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[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boraston, A B]]
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[[Category: Boraston AB]]
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[[Category: Pluvinage, B]]
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[[Category: Pluvinage B]]
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[[Category: Carbohydrate binding module]]
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[[Category: Sugar binding protein]]
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Current revision

Crystal structure of Br derivative BhCBM56

PDB ID 5t7a

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