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| | <StructureSection load='6bsv' size='340' side='right'caption='[[6bsv]], [[Resolution|resolution]] 2.43Å' scene=''> | | <StructureSection load='6bsv' size='340' side='right'caption='[[6bsv]], [[Resolution|resolution]] 2.43Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BSV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bsv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BSV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 2.433Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XXT1, XT1, At3g62720, F26K9_150 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Xyloglucan_6-xylosyltransferase Xyloglucan 6-xylosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.39 2.4.2.39] </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=6bsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bsv OCA], [https://pdbe.org/6bsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bsv RCSB], [https://www.ebi.ac.uk/pdbsum/6bsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bsv 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=6bsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bsv OCA], [https://pdbe.org/6bsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bsv RCSB], [https://www.ebi.ac.uk/pdbsum/6bsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bsv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/XXT1_ARATH XXT1_ARATH]] Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues.<ref>PMID:12032363</ref> <ref>PMID:16982611</ref> <ref>PMID:18544630</ref>
| + | [https://www.uniprot.org/uniprot/XXT1_ARATH XXT1_ARATH] Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues.<ref>PMID:12032363</ref> <ref>PMID:16982611</ref> <ref>PMID:18544630</ref> |
| | <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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xyloglucan 6-xylosyltransferase]]
| + | [[Category: Choe J]] |
| - | [[Category: Choe, J]] | + | [[Category: Culbertson AT]] |
| - | [[Category: Culbertson, A T]] | + | [[Category: Ehrlich JJ]] |
| - | [[Category: Ehrlich, J J]] | + | [[Category: Honzatko RB]] |
| - | [[Category: Honzatko, R B]] | + | [[Category: Zabotina OA]] |
| - | [[Category: Zabotina, O A]] | + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xyloglucan]]
| + | |
| - | [[Category: Xylosyltransferase]]
| + | |
| Structural highlights
Function
XXT1_ARATH Xylosyltransferase specific to UDP-D-xylose that accepts both cellopentaose and cellohexaose as substrates, with a better use of cellohexaose, to produce xyloglucan. Adds preferentially the first xylosyl residue to the fourth glucosyl residue from the reducing end of both acceptors. Transfer one xylose mainly to the second glucose residue from the non-reducing end. The acceptor should have a minimum of four glucose residues.[1] [2] [3]
Publication Abstract from PubMed
The plant cell wall is primarily a polysaccharide mesh of the most abundant biopolymers on earth. Although one of the richest sources of biorenewable materials, the biosynthesis of the plant polysaccharides is poorly understood. Structures of many essential plant glycosyltransferases are unknown and suitable substrates are often unavailable for in vitro analysis. The dearth of such information impedes the development of plants better suited for industrial applications. Presented here are structures of Arabidopsis xyloglucan xylosyltransferase 1 (XXT1) without ligands and in complexes with UDP and cellohexaose. XXT1 initiates side-chain extensions from a linear glucan polymer by transferring the xylosyl group from UDP-xylose during xyloglucan biosynthesis. XXT1, a homodimer and member of the GT-A fold family of glycosyltransferases, binds UDP analogously to other GT-A fold enzymes. Structures here and the properties of mutant XXT1s are consistent with a SNi-like catalytic mechanism. Distinct from other systems is the recognition of cellohexaose by way of an extended cleft. The XXT1 dimer alone cannot produce xylosylation patterns observed for native xyloglucans because of steric constraints imposed by the acceptor binding cleft. Homology modeling of XXT2 and XXT5, the other two xylosyltransferases involved in xyloglucan biosynthesis, reveals a structurally altered cleft in XXT5 that could accommodate a partially xylosylated glucan chain produced by XXT1 and/or XXT2. An assembly of the three XXTs can produce the xylosylation patterns of native xyloglucans, suggesting the involvement of an organized multienzyme complex in the xyloglucan biosynthesis.
Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers.,Culbertson AT, Ehrlich JJ, Choe JY, Honzatko RB, Zabotina OA Proc Natl Acad Sci U S A. 2018 May 21. pii: 1801105115. doi:, 10.1073/pnas.1801105115. PMID:29784804[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Faik A, Price NJ, Raikhel NV, Keegstra K. An Arabidopsis gene encoding an alpha-xylosyltransferase involved in xyloglucan biosynthesis. Proc Natl Acad Sci U S A. 2002 May 28;99(11):7797-802. doi:, 10.1073/pnas.102644799. PMID:12032363 doi:http://dx.doi.org/10.1073/pnas.102644799
- ↑ Cavalier DM, Keegstra K. Two xyloglucan xylosyltransferases catalyze the addition of multiple xylosyl residues to cellohexaose. J Biol Chem. 2006 Nov 10;281(45):34197-207. doi: 10.1074/jbc.M606379200. Epub, 2006 Sep 18. PMID:16982611 doi:http://dx.doi.org/10.1074/jbc.M606379200
- ↑ Cavalier DM, Lerouxel O, Neumetzler L, Yamauchi K, Reinecke A, Freshour G, Zabotina OA, Hahn MG, Burgert I, Pauly M, Raikhel NV, Keegstra K. Disrupting two Arabidopsis thaliana xylosyltransferase genes results in plants deficient in xyloglucan, a major primary cell wall component. Plant Cell. 2008 Jun;20(6):1519-37. doi: 10.1105/tpc.108.059873. Epub 2008 Jun, 10. PMID:18544630 doi:http://dx.doi.org/10.1105/tpc.108.059873
- ↑ Culbertson AT, Ehrlich JJ, Choe JY, Honzatko RB, Zabotina OA. Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers. Proc Natl Acad Sci U S A. 2018 May 21. pii: 1801105115. doi:, 10.1073/pnas.1801105115. PMID:29784804 doi:http://dx.doi.org/10.1073/pnas.1801105115
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