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5foe

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Revision as of 13:35, 15 March 2017

Crystal structure of the C. elegans Protein O-fucosyltransferase 2 (CePOFUT2) double mutant (R298K-R299K) in complex with GDP and the human TSR1 from thrombospondin 1

Structural highlights

5foe is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Peptide-O-fucosyltransferase, with EC number 2.4.1.221
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OFUT2_CAEEL] Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13 (By similarity).^[1]

Publication Abstract from PubMed

Protein O-fucosyltransferase 2 (POFUT2) is an essential enzyme that fucosylates serine and threonine residues of folded thrombospondin type 1 repeats (TSRs). To date, the mechanism by which this enzyme recognizes very dissimilar TSRs has been unclear. By engineering a fusion protein, we report the crystal structure of Caenorhabditis elegans POFUT2 (CePOFUT2) in complex with GDP and human TSR1 that suggests an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the TSR1 is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex. Site-directed mutagenesis demonstrates that POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-C. Crystallographic and mutagenesis data, together with atomic-level simulations, uncover a binding mechanism by which POFUT2 promiscuously recognizes the structural fingerprint of poorly homologous TSRs through a dynamic network of water-mediated interactions.

A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2.,Valero-Gonzalez J, Leonhard-Melief C, Lira-Navarrete E, Jimenez-Oses G, Hernandez-Ruiz C, Pallares MC, Yruela I, Vasudevan D, Lostao A, Corzana F, Takeuchi H, Haltiwanger RS, Hurtado-Guerrero R Nat Chem Biol. 2016 Feb 8. doi: 10.1038/nchembio.2019. PMID:26854667^[2]

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

References

↑ Menzel O, Vellai T, Takacs-Vellai K, Reymond A, Mueller F, Antonarakis SE, Guipponi M. The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development. Genomics. 2004 Aug;84(2):320-30. PMID:15233996 doi:http://dx.doi.org/10.1016/j.ygeno.2004.04.002
↑ Valero-Gonzalez J, Leonhard-Melief C, Lira-Navarrete E, Jimenez-Oses G, Hernandez-Ruiz C, Pallares MC, Yruela I, Vasudevan D, Lostao A, Corzana F, Takeuchi H, Haltiwanger RS, Hurtado-Guerrero R. A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2. Nat Chem Biol. 2016 Feb 8. doi: 10.1038/nchembio.2019. PMID:26854667 doi:http://dx.doi.org/10.1038/nchembio.2019

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/5foe"

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[5foe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FOE FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5foe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5foe OCA], [http://pdbe.org/5foe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5foe RCSB], [http://www.ebi.ac.uk/pdbsum/5foe PDBsum]</span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-O-fucosyltransferase Peptide-O-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.221 2.4.1.221] </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=5foe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5foe OCA], [http://pdbe.org/5foe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5foe RCSB], [http://www.ebi.ac.uk/pdbsum/5foe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5foe ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Peptide-O-fucosyltransferase]]
 [[Category: Corzana, F]]
 [[Category: Haltiwanger, R S]]

5foe

From Proteopedia

Revision as of 13:35, 15 March 2017

Crystal structure of the C. elegans Protein O-fucosyltransferase 2 (CePOFUT2) double mutant (R298K-R299K) in complex with GDP and the human TSR1 from thrombospondin 1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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