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| | <StructureSection load='4ayg' size='340' side='right'caption='[[4ayg]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4ayg' size='340' side='right'caption='[[4ayg]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ayg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_23272 Atcc 23272]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AYG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ayg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limosilactobacillus_reuteri Limosilactobacillus reuteri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ayg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayg OCA], [http://pdbe.org/4ayg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ayg RCSB], [http://www.ebi.ac.uk/pdbsum/4ayg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayg ProSAT]</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=4ayg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayg OCA], [https://pdbe.org/4ayg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayg RCSB], [https://www.ebi.ac.uk/pdbsum/4ayg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5SBN3_LIMRT Q5SBN3_LIMRT] Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.[ARBA:ARBA00003243] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 23272]] | + | [[Category: Large Structures]] |
| - | [[Category: Dextransucrase]] | + | [[Category: Limosilactobacillus reuteri]] |
| - | [[Category: Dijkhuizen, L]] | + | [[Category: Dijkhuizen L]] |
| - | [[Category: Dijkstra, B W]] | + | [[Category: Dijkstra BW]] |
| - | [[Category: Kralj, S]] | + | [[Category: Kralj S]] |
| - | [[Category: Pijning, T]] | + | [[Category: Pijning T]] |
| - | [[Category: Vujicic-Zagar, A]] | + | [[Category: Vujicic-Zagar A]] |
| - | [[Category: Circularly permuted beta-alpha barrel]]
| + | |
| - | [[Category: Glycosyl hydrolase family 70]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
4ayg is a 2 chain structure with sequence from Limosilactobacillus reuteri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q5SBN3_LIMRT Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.[ARBA:ARBA00003243]
Publication Abstract from PubMed
Glucansucrase enzymes synthesize high-molecular-mass extracellular alpha-glucan polysaccharides from sucrose. Previously, the crystal structure of truncated glucansucrase glucosyltransferase (GTF)180-DeltaN from Lactobacillus reuteri 180 (lacking the N-terminal domain) revealed an elongated overall structure with two remote domains (IV and V) extending away from the core. By contrast, a new crystal form of the alpha-1,6/alpha-1,3 specific glucansucrase GTF180-DeltaN shows an approximate 120o rotation of domain V about a hinge located between domains IV and V, giving a much more compact structure than before. Positional variability of domain V in solution is confirmed by small angle X-ray scattering experiments and rigid-body ensemble calculations. In addition, small angle X-ray scattering measurements of full-length GTF180 also provide the first structural data for a full-length glucansucrase, showing that the enzyme has an almost symmetric boomerang-like molecular shape, with a bend likely located between domains IV and V. The ~ 700-residue N-terminal domain, which is not present in the crystal structures, extends away from domain V and the catalytic core of the enzyme. We conclude that, as a result of the hinge region, in solution, GTF180-DeltaN (and likely also the full-length GTF180) shows conformational flexibility; this may be a general feature of GH70 glucansucrases. DATABASE: * Structural data for GTF180-DeltaN II have been deposited in the Protein Data Bank under accession code 4AYG.
Flexibility of truncated and full-length glucansucrase GTF180 enzymes from Lactobacillus reuteri 180.,Pijning T, Vujicic-Zagar A, Kralj S, Dijkhuizen L, Dijkstra BW FEBS J. 2014 Mar 6. doi: 10.1111/febs.12769. PMID:24597929[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pijning T, Vujicic-Zagar A, Kralj S, Dijkhuizen L, Dijkstra BW. Flexibility of truncated and full-length glucansucrase GTF180 enzymes from Lactobacillus reuteri 180. FEBS J. 2014 Mar 6. doi: 10.1111/febs.12769. PMID:24597929 doi:http://dx.doi.org/10.1111/febs.12769
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