5kor

From Proteopedia

(Difference between revisions)

Current revision

Arabidopsis thaliana fucosyltransferase 1 (FUT1) in complex with GDP and a xylo-oligossacharide

Structural highlights

5kor is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUT1_ARATH Involved in cell wall biosynthesis. Is both necessary and sufficient for the addition of the terminal fucosyl residue on xyloglucan side chains, but is not involved in the fucosylation of other cell wall components (PubMed:10373113, PubMed:11743104, PubMed:11854459, PubMed:14730072). Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi (PubMed:25392066).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

The plant cell wall is a complex and dynamic network made mostly of cellulose, hemicelluloses and pectins. Xyloglucan, the major hemicellulosic component in Arabidopsis thaliana, is biosynthesized in the Golgi apparatus by a series of glycan synthases and glycosyltransferases before export to the wall. A better understanding of the xyloglucan biosynthetic machinery will give clues toward engineering plants with improved wall properties or designing novel xyloglucan-based biomaterials. The xyloglucan-specific alpha-2-fucosyltransferase FUT1 catalyzes the transfer of fucose from GDP-fucose to terminal galactosyl residues on xyloglucan side chains. Here, we present crystal structures of Arabidopsis FUT1 in its apoform and in a ternary complex with GDP and a xylo-oligosaccharide acceptor (named XLLG). Although FUT1 is clearly a member of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a variant of the GT-B fold. In particular, it includes an extra C-terminal region that is part of the acceptor binding site. Our crystal structures support previous findings that FUT1 behaves as a functional dimer. Mutational studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a SN2-like reaction mechanism similar to that of protein-O-fucosyltransferase 2. Thus, our results provide new insights into the mechanism of xyloglucan fucosylation in the Golgi.

Structure of Arabidopsis thaliana FUT1 Reveals a Variant of the GT-B Class Fold and Provides Insight into Xyloglucan Fucosylation.,Rocha J, Ciceron F, de Sanctis D, Lelimousin M, Chazalet V, Lerouxel O, Breton C Plant Cell. 2016 Sep 16. pii: tpc.00519.2016. PMID:27637560^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Perrin RM, DeRocher AE, Bar-Peled M, Zeng W, Norambuena L, Orellana A, Raikhel NV, Keegstra K. Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall biosynthesis. Science. 1999 Jun 18;284(5422):1976-9. PMID:10373113
↑ Sarria R, Wagner TA, O'Neill MA, Faik A, Wilkerson CG, Keegstra K, Raikhel NV. Characterization of a family of Arabidopsis genes related to xyloglucan fucosyltransferase1. Plant Physiol. 2001 Dec;127(4):1595-606. PMID:11743104
↑ Vanzin GF, Madson M, Carpita NC, Raikhel NV, Keegstra K, Reiter WD. The mur2 mutant of Arabidopsis thaliana lacks fucosylated xyloglucan because of a lesion in fucosyltransferase AtFUT1. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):3340-5. Epub 2002 Feb 19. PMID:11854459 doi:http://dx.doi.org/10.1073/pnas.052450699
↑ Pena MJ, Ryden P, Madson M, Smith AC, Carpita NC. The galactose residues of xyloglucan are essential to maintain mechanical strength of the primary cell walls in Arabidopsis during growth. Plant Physiol. 2004 Jan;134(1):443-51. PMID:14730072 doi:http://dx.doi.org/10.1104/pp.103.027508
↑ Chou YH, Pogorelko G, Young ZT, Zabotina OA. Protein-protein interactions among xyloglucan-synthesizing enzymes and formation of Golgi-localized multiprotein complexes. Plant Cell Physiol. 2015 Feb;56(2):255-67. doi: 10.1093/pcp/pcu161. Epub 2014 Nov, 11. PMID:25392066 doi:http://dx.doi.org/10.1093/pcp/pcu161
↑ Rocha J, Ciceron F, de Sanctis D, Lelimousin M, Chazalet V, Lerouxel O, Breton C. Structure of Arabidopsis thaliana FUT1 Reveals a Variant of the GT-B Class Fold and Provides Insight into Xyloglucan Fucosylation. Plant Cell. 2016 Sep 16. pii: tpc.00519.2016. PMID:27637560 doi:http://dx.doi.org/10.1105/tpc.16.00519

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kor"

Categories: Arabidopsis thaliana | Large Structures | Breton C | Rocha J | De Sanctis D

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5kor is ON HOLD
+==Arabidopsis thaliana fucosyltransferase 1 (FUT1) in complex with GDP and a xylo-oligossacharide==
+<StructureSection load='5kor' size='340' side='right'caption='[[5kor]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5kor]] is a 4 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=5KOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></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=5kor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kor OCA], [https://pdbe.org/5kor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kor RCSB], [https://www.ebi.ac.uk/pdbsum/5kor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kor ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUT1_ARATH FUT1_ARATH] Involved in cell wall biosynthesis. Is both necessary and sufficient for the addition of the terminal fucosyl residue on xyloglucan side chains, but is not involved in the fucosylation of other cell wall components (PubMed:10373113, PubMed:11743104, PubMed:11854459, PubMed:14730072). Associates with other xyloglucan-synthesizing enzymes to form multiprotein complexes for xyloglucan synthesis in the Golgi (PubMed:25392066).<ref>PMID:10373113</ref> <ref>PMID:11743104</ref> <ref>PMID:11854459</ref> <ref>PMID:14730072</ref> <ref>PMID:25392066</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The plant cell wall is a complex and dynamic network made mostly of cellulose, hemicelluloses and pectins. Xyloglucan, the major hemicellulosic component in Arabidopsis thaliana, is biosynthesized in the Golgi apparatus by a series of glycan synthases and glycosyltransferases before export to the wall. A better understanding of the xyloglucan biosynthetic machinery will give clues toward engineering plants with improved wall properties or designing novel xyloglucan-based biomaterials. The xyloglucan-specific alpha-2-fucosyltransferase FUT1 catalyzes the transfer of fucose from GDP-fucose to terminal galactosyl residues on xyloglucan side chains. Here, we present crystal structures of Arabidopsis FUT1 in its apoform and in a ternary complex with GDP and a xylo-oligosaccharide acceptor (named XLLG). Although FUT1 is clearly a member of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a variant of the GT-B fold. In particular, it includes an extra C-terminal region that is part of the acceptor binding site. Our crystal structures support previous findings that FUT1 behaves as a functional dimer. Mutational studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a SN2-like reaction mechanism similar to that of protein-O-fucosyltransferase 2. Thus, our results provide new insights into the mechanism of xyloglucan fucosylation in the Golgi.
-Authors:
+Structure of Arabidopsis thaliana FUT1 Reveals a Variant of the GT-B Class Fold and Provides Insight into Xyloglucan Fucosylation.,Rocha J, Ciceron F, de Sanctis D, Lelimousin M, Chazalet V, Lerouxel O, Breton C Plant Cell. 2016 Sep 16. pii: tpc.00519.2016. PMID:27637560<ref>PMID:27637560</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5kor" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Breton C]]
+[[Category: Rocha J]]
+[[Category: De Sanctis D]]

5kor

From Proteopedia

Current revision

Arabidopsis thaliana fucosyltransferase 1 (FUT1) in complex with GDP and a xylo-oligossacharide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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