3ttq: Difference between revisions

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<StructureSection load='3ttq' size='340' side='right'caption='[[3ttq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3ttq' size='340' side='right'caption='[[3ttq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ttq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ascococcus_mesenteroides"_tsenkovskii_1878 "ascococcus mesenteroides" tsenkovskii 1878]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TTQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ttq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TTQ FirstGlance]. <br>
</td></tr><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tto|3tto]]</div></td></tr>
<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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsr-E, dsrE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 "Ascococcus mesenteroides" Tsenkovskii 1878])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </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=3ttq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ttq OCA], [https://pdbe.org/3ttq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ttq RCSB], [https://www.ebi.ac.uk/pdbsum/3ttq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ttq 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=3ttq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ttq OCA], [https://pdbe.org/3ttq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ttq RCSB], [https://www.ebi.ac.uk/pdbsum/3ttq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ttq ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8G9Q2_LEUME Q8G9Q2_LEUME]
DeltaN(123)-glucan-binding domain-catalytic domain 2 (DeltaN(123)-GBD-CD2) is a truncated form of the bifunctional glucansucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299. It was constructed by rational truncation of GBD-CD2, which harbors the second catalytic domain of DSR-E. Like GBD-CD2, this variant displays alpha-(1--&gt;2) branching activity when incubated with sucrose as glucosyl donor and (oligo-)dextran as acceptor, transferring glucosyl residues to the acceptor via a ping-pong bi-bi mechanism. This allows the formation of prebiotic molecules containing controlled amounts of alpha-(1--&gt;2) linkages. The crystal structure of the apo alpha-(1--&gt;2) branching sucrase DeltaN(123)-GBD-CD2 was solved at 1.90 A resolution. The protein adopts the unusual U-shape fold organized in five distinct domains, also found in GTF180-DeltaN and GTF-SI glucansucrases of glycoside hydrolase family 70. Residues forming subsite -1, involved in binding the glucosyl residue of sucrose and catalysis, are strictly conserved in both GTF180-DeltaN and DeltaN(123)-GBD-CD2. Subsite +1 analysis revealed three residues (Ala-2249, Gly-2250, and Phe-2214) that are specific to DeltaN(123)-GBD-CD2. Mutation of these residues to the corresponding residues found in GTF180-DeltaN showed that Ala-2249 and Gly-2250 are not directly involved in substrate binding and regiospecificity. In contrast, mutant F2214N had lost its ability to branch dextran, although it was still active on sucrose alone. Furthermore, three loops belonging to domains A and B at the upper part of the catalytic gorge are also specific to DeltaN(123)-GBD-CD2. These distinguishing features are also proposed to be involved in the correct positioning of dextran acceptor molecules allowing the formation of alpha-(1--&gt;2) branches.
 
Functional and structural characterization of alpha-(1-&gt;2) branching sucrase derived from DSR-E glucansucrase.,Brison Y, Pijning T, Malbert Y, Fabre E, Mourey L, Morel S, Potocki-Veronese G, Monsan P, Tranier S, Remaud-Simeon M, Dijkstra BW J Biol Chem. 2012 Mar 9;287(11):7915-24. Epub 2012 Jan 18. PMID:22262856<ref>PMID:22262856</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ttq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ascococcus mesenteroides tsenkovskii 1878]]
[[Category: Dextransucrase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brison, Y]]
[[Category: Leuconostoc mesenteroides]]
[[Category: Dijkstra, B W]]
[[Category: Brison Y]]
[[Category: Fabre, E]]
[[Category: Dijkstra BW]]
[[Category: Monsan, P]]
[[Category: Fabre E]]
[[Category: Morel, S]]
[[Category: Monsan P]]
[[Category: Mourey, L]]
[[Category: Morel S]]
[[Category: Pijning, T]]
[[Category: Mourey L]]
[[Category: Potocki-Veronese, G]]
[[Category: Pijning T]]
[[Category: Remaud-Simeon, M]]
[[Category: Potocki-Veronese G]]
[[Category: Tranier, S]]
[[Category: Remaud-Simeon M]]
[[Category: Branching dextransucrase]]
[[Category: Tranier S]]
[[Category: Alpha-1]]
[[Category: Sucrose/dextran/gluco-oligosaccharide binding]]
[[Category: Transferase]]

Latest revision as of 16:39, 14 March 2024

Crystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in orthorhombic apo-form at 1.9 angstrom resolutionCrystal structure of Leuconostoc mesenteroides NRRL B-1299 N-terminally truncated dextransucrase DSR-E in orthorhombic apo-form at 1.9 angstrom resolution

Structural highlights

3ttq is a 1 chain structure with sequence from Leuconostoc mesenteroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8G9Q2_LEUME

3ttq, resolution 1.90Å

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OCA
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