5koe

From Proteopedia

(Difference between revisions)

Current revision

The structure of Arabidopsis thaliana FUT1 in complex with XXLG

Structural highlights

5koe 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 1.79Å
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 mechanistic underpinnings of the complex process of plant polysaccharide biosynthesis are poorly understood, largely because of the resistance of glycosyltransferase (GT) enzymes to structural characterization. In Arabidopsis thaliana, a glycosyl transferase family 37 (GT37) fucosyltransferase 1 (AtFUT1) catalyzes the regiospecific transfer of terminal 1,2-fucosyl residues to xyloglucan side chains - a key step in the biosynthesis of fucosylated sidechains of galactoxyloglucan. We unravel the mechanistic basis for fucosylation by AtFUT1 with a multipronged approach involving protein expression, X-ray crystallography, mutagenesis experiments and molecular simulations. Mammalian cell culture expressions enable the sufficient production of the enzyme for X-ray crystallography, which reveals the structural architecture of AtFUT1 in complex with bound donor and acceptor substrate analogs. The lack of an appropriately positioned active site residue as a catalytic base leads us to propose an atypical water-mediated fucosylation mechanism facilitated by an H-bonded network, which is corroborated by mutagenesis experiments as well as detailed atomistic simulations.

Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism.,Urbanowicz BR, Bharadwaj VS, Alahuhta M, Pena MJ, Lunin VV, Bomble YJ, Wang S, Yang JY, Tuomivaara ST, Himmel ME, Moremen KW, York WS, Crowley MF Plant J. 2017 Sep;91(6):931-949. doi: 10.1111/tpj.13628. Epub 2017 Aug 28. PMID:28670741^[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
↑ Urbanowicz BR, Bharadwaj VS, Alahuhta M, Pena MJ, Lunin VV, Bomble YJ, Wang S, Yang JY, Tuomivaara ST, Himmel ME, Moremen KW, York WS, Crowley MF. Structural, mutagenic and in silico studies of xyloglucan fucosylation in Arabidopsis thaliana suggest a water-mediated mechanism. Plant J. 2017 Sep;91(6):931-949. doi: 10.1111/tpj.13628. Epub 2017 Aug 28. PMID:28670741 doi:http://dx.doi.org/10.1111/tpj.13628

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/5koe"

Categories: Arabidopsis thaliana | Large Structures | Alahuhta PM | Lunin VV

@@ Line 1: / Line 1: @@
 ==The structure of Arabidopsis thaliana FUT1 in complex with XXLG==
-<StructureSection load='5koe' size='340' side='right' caption='[[5koe]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+<StructureSection load='5koe' size='340' side='right'caption='[[5koe]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5koe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5koe]] 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=5KOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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]] 1.79&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FUT1, FT1, MUR2, At2g03220, T18E12.11 ([http://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=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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactoside_2-alpha-L-fucosyltransferase Galactoside 2-alpha-L-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.69 2.4.1.69] </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=5koe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5koe OCA], [https://pdbe.org/5koe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5koe RCSB], [https://www.ebi.ac.uk/pdbsum/5koe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5koe ProSAT]</span></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=5koe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5koe OCA], [http://pdbe.org/5koe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5koe RCSB], [http://www.ebi.ac.uk/pdbsum/5koe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5koe ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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 ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
-[[Category: Galactoside 2-alpha-L-fucosyltransferase]]
-[[Category: Alahuhta, P M]]
-[[Category: Lunin, V V]]
-[[Category: Acetyl transferase]]
 [[Category: Arabidopsis thaliana]]
-[[Category: Cell adhesion]]
+[[Category: Large Structures]]
-[[Category: Gt37]]
+[[Category: Alahuhta PM]]
-[[Category: Xxlg]]
+[[Category: Lunin VV]]

5koe

From Proteopedia

Current revision

The structure of Arabidopsis thaliana FUT1 in complex with XXLG

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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