5x7s

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==Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative==
==Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative==
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<StructureSection load='5x7s' size='340' side='right' caption='[[5x7s]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5x7s' size='340' side='right'caption='[[5x7s]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x7s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paenibacillus_sp._598k Paenibacillus sp. 598k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X7S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x7s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_sp._598K Paenibacillus sp. 598K]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X7S 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</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]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x7o|5x7o]], [[5x7p|5x7p]], [[5x7q|5x7q]], [[5x7r|5x7r]], [[5x7g|5x7g]], [[5x7h|5x7h]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">6gt31a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1117987 Paenibacillus sp. 598K])</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=5x7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x7s OCA], [https://pdbe.org/5x7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x7s RCSB], [https://www.ebi.ac.uk/pdbsum/5x7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x7s ProSAT]</span></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=5x7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x7s OCA], [http://pdbe.org/5x7s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x7s RCSB], [http://www.ebi.ac.uk/pdbsum/5x7s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x7s ProSAT]</span></td></tr>
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</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/A0A193PKW5_9BACL A0A193PKW5_9BACL]
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Paenibacillus sp. 598K alpha-1,6-glucosyltransferase (Ps6TG31A), a member of glycoside hydrolase family 31, catalyzes exo-alpha-glucohydrolysis and transglucosylation and produces alpha-1,6-glucosyl-alpha-glucosaccharides from alpha-glucan via its disproportionation activity. The crystal structure of Ps6TG31A was determined by an anomalous dispersion method using a terbium derivative. The monomeric Ps6TG31A consisted of one catalytic (beta/alpha)8-barrel domain and six small domains, one on the N-terminal and five on the C-terminal side. The structures of the enzyme complexed with maltohexaose, isomaltohexaose, and acarbose demonstrated that the ligands were observed in the catalytic cleft and the sugar-binding sites of four beta-domains. The catalytic site was structured by a glucose-binding pocket and an aglycon-binding cleft built by two sidewalls. The bound acarbose was located with its non-reducing end pseudosugar docked in the pocket, and the other moieties along one sidewall serving three subsites for the alpha-1,4-glucan. The bound isomaltooligosaccharide was found on the opposite sidewall, which provided the space for the acceptor molecule to be positioned for attack of the catalytic intermediate covalent complex during transglucosylation. The N-terminal domain recognized the alpha-1,4-glucan in a surface-binding mode. Two of the five C-terminal domains belong to the carbohydrate-binding modules family 35 and one to family 61. The sugar complex structures indicated that the first family 35 module preferred alpha-1,6-glucan, whereas the second family 35 module and family 61 module preferred alpha-1,4-glucan. Ps6TG31A appears to have enhanced transglucosylation activity facilitated by its carbohydrate-binding modules and substrate-binding cleft that positions the substrate and acceptor sugar for the transglucosylation.
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Carbohydrate-binding architecture of the multi-modular alpha-1,6-glucosyltransferase from Paenibacillus sp. 598K, which produces alpha-1,6-glucosyl-alpha-glucosaccharides from starch.,Fujimoto Z, Suzuki N, Kishine N, Ichinose H, Momma M, Kimura A, Funane K Biochem J. 2017 Aug 7;474(16):2763-2778. doi: 10.1042/BCJ20170152. PMID:28698247<ref>PMID:28698247</ref>
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==See Also==
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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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 5x7s" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Paenibacillus sp. 598k]]
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[[Category: Large Structures]]
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[[Category: Fujimoto, Z]]
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[[Category: Paenibacillus sp. 598K]]
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[[Category: Funane, K]]
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[[Category: Fujimoto Z]]
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[[Category: Ichinose, H]]
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[[Category: Funane K]]
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[[Category: Kimura, A]]
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[[Category: Ichinose H]]
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[[Category: Kishine, N]]
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[[Category: Kimura A]]
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[[Category: Momma, M]]
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[[Category: Kishine N]]
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[[Category: Suzuki, N]]
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[[Category: Momma M]]
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[[Category: Carbohydrate-binding module family 35]]
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[[Category: Suzuki N]]
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[[Category: Carbohydrate-binding module family 61]]
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[[Category: Glydoside hydrolase family 31]]
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[[Category: Hydrolase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative

PDB ID 5x7s

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