5kop: Difference between revisions

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==Arabidopsis thaliana fucosyltransferase 1 (FUT1) in its apo-form==
==Arabidopsis thaliana fucosyltransferase 1 (FUT1) in its apo-form==
<StructureSection load='5kop' size='340' side='right' caption='[[5kop]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5kop' size='340' side='right'caption='[[5kop]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5kop]] 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=5KOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOP FirstGlance]. <br>
<table><tr><td colspan='2'>[[5kop]] 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=5KOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.1&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5kop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kop OCA], [https://pdbe.org/5kop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kop RCSB], [https://www.ebi.ac.uk/pdbsum/5kop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kop 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=5kop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kop OCA], [http://pdbe.org/5kop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kop RCSB], [http://www.ebi.ac.uk/pdbsum/5kop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kop ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>  
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<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: Galactoside 2-alpha-L-fucosyltransferase]]
[[Category: Large Structures]]
[[Category: Breton, C]]
[[Category: Breton C]]
[[Category: Rocha, J]]
[[Category: Rocha J]]
[[Category: Sanctis, D de]]
[[Category: De Sanctis D]]
[[Category: Apo-form]]
[[Category: Fucosyltransferase]]
[[Category: Golgi]]
[[Category: Transferase]]

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