8d0x: Difference between revisions

Revision as of 04:03, 25 May 2023

Human FUT9 bound to LNnT

Structural highlights

8d0x is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	BMA, EDO, GAL, GOL, MAN, NAG, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FUT9_HUMAN Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth (PubMed:23263199, PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574, PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078, PubMed:16282604, PubMed:29593094). Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (PubMed:12107078, PubMed:18395013). Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (PubMed:18395013, PubMed:23192350). May also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10]

References

↑ Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H. Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. FEBS Lett. 1999 Jun 11;452(3):237-42. PMID:10386598 doi:10.1016/s0014-5793(99)00640-7
↑ Nishihara S, Iwasaki H, Kaneko M, Tawada A, Ito M, Narimatsu H. Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue. FEBS Lett. 1999 Dec 3;462(3):289-94. PMID:10622713 doi:10.1016/s0014-5793(99)01549-5
↑ Nakayama F, Nishihara S, Iwasaki H, Kudo T, Okubo R, Kaneko M, Nakamura M, Karube M, Sasaki K, Narimatsu H. CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV. J Biol Chem. 2001 May 11;276(19):16100-6. PMID:11278338 doi:10.1074/jbc.M007272200
↑ Toivonen S, Nishihara S, Narimatsu H, Renkonen O, Renkonen R. Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor site-specificity profile. Glycobiology. 2002 Jun;12(6):361-8. PMID:12107078 doi:10.1093/glycob/12.6.361
↑ Bogoevska V, Horst A, Klampe B, Lucka L, Wagener C, Nollau P. CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues. Glycobiology. 2006 Mar;16(3):197-209. PMID:16282604 doi:10.1093/glycob/cwj057
↑ Brito C, Escrevente C, Reis CA, Lee VM, Trojanowski JQ, Costa J. Increased levels of fucosyltransferase IX and carbohydrate Lewis(x) adhesion determinant in human NT2N neurons. J Neurosci Res. 2007 May 1;85(6):1260-70. PMID:17335083 doi:10.1002/jnr.21230
↑ Brito C, Kandzia S, Graça T, Conradt HS, Costa J. Human fucosyltransferase IX: specificity towards N-linked glycoproteins and relevance of the cytoplasmic domain in intra-Golgi localization. Biochimie. 2008 Sep;90(9):1279-90. PMID:18395013 doi:10.1016/j.biochi.2008.03.002
↑ Gouveia R, Schaffer L, Papp S, Grammel N, Kandzia S, Head SR, Kleene R, Schachner M, Conradt HS, Costa J. Expression of glycogenes in differentiating human NT2N neurons. Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels and impaired neurite outgrowth. Biochim Biophys Acta. 2012 Dec;1820(12):2007-19. PMID:23000574 doi:10.1016/j.bbagen.2012.09.004
↑ Buffone A Jr, Mondal N, Gupta R, McHugh KP, Lau JT, Neelamegham S. Silencing α1,3-fucosyltransferases in human leukocytes reveals a role for FUT9 enzyme during E-selectin-mediated cell adhesion. J Biol Chem. 2013 Jan 18;288(3):1620-33. PMID:23192350 doi:10.1074/jbc.M112.400929
↑ Seelhorst K, Stacke C, Ziegelmüller P, Hahn U. N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity. Glycobiology. 2013 May;23(5):559-67. PMID:23263199 doi:10.1093/glycob/cws219

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OCA

[1] Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H. Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. FEBS Lett. 1999 Jun 11;452(3):237-42. PMID:10386598 doi:10.1016/s0014-5793(99)00640-7

[2] Nishihara S, Iwasaki H, Kaneko M, Tawada A, Ito M, Narimatsu H. Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue. FEBS Lett. 1999 Dec 3;462(3):289-94. PMID:10622713 doi:10.1016/s0014-5793(99)01549-5

[3] Nakayama F, Nishihara S, Iwasaki H, Kudo T, Okubo R, Kaneko M, Nakamura M, Karube M, Sasaki K, Narimatsu H. CD15 expression in mature granulocytes is determined by alpha 1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-fucosyltransferase IV. J Biol Chem. 2001 May 11;276(19):16100-6. PMID:11278338 doi:10.1074/jbc.M007272200

[4] Toivonen S, Nishihara S, Narimatsu H, Renkonen O, Renkonen R. Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct acceptor site-specificity profile. Glycobiology. 2002 Jun;12(6):361-8. PMID:12107078 doi:10.1093/glycob/12.6.361

[5] Bogoevska V, Horst A, Klampe B, Lucka L, Wagener C, Nollau P. CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues. Glycobiology. 2006 Mar;16(3):197-209. PMID:16282604 doi:10.1093/glycob/cwj057

[6] Brito C, Escrevente C, Reis CA, Lee VM, Trojanowski JQ, Costa J. Increased levels of fucosyltransferase IX and carbohydrate Lewis(x) adhesion determinant in human NT2N neurons. J Neurosci Res. 2007 May 1;85(6):1260-70. PMID:17335083 doi:10.1002/jnr.21230

[7] Brito C, Kandzia S, Graça T, Conradt HS, Costa J. Human fucosyltransferase IX: specificity towards N-linked glycoproteins and relevance of the cytoplasmic domain in intra-Golgi localization. Biochimie. 2008 Sep;90(9):1279-90. PMID:18395013 doi:10.1016/j.biochi.2008.03.002

[8] Gouveia R, Schaffer L, Papp S, Grammel N, Kandzia S, Head SR, Kleene R, Schachner M, Conradt HS, Costa J. Expression of glycogenes in differentiating human NT2N neurons. Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels and impaired neurite outgrowth. Biochim Biophys Acta. 2012 Dec;1820(12):2007-19. PMID:23000574 doi:10.1016/j.bbagen.2012.09.004

[9] Buffone A Jr, Mondal N, Gupta R, McHugh KP, Lau JT, Neelamegham S. Silencing α1,3-fucosyltransferases in human leukocytes reveals a role for FUT9 enzyme during E-selectin-mediated cell adhesion. J Biol Chem. 2013 Jan 18;288(3):1620-33. PMID:23192350 doi:10.1074/jbc.M112.400929

[10] Seelhorst K, Stacke C, Ziegelmüller P, Hahn U. N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity. Glycobiology. 2013 May;23(5):559-67. PMID:23263199 doi:10.1093/glycob/cws219

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8d0x is ON HOLD  until Paper Publication
+==Human FUT9 bound to LNnT==
+<StructureSection load='8d0x' size='340' side='right'caption='[[8d0x]], [[Resolution|resolution]] 1.33&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8d0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D0X FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d0x OCA], [https://pdbe.org/8d0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d0x RCSB], [https://www.ebi.ac.uk/pdbsum/8d0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d0x ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUT9_HUMAN FUT9_HUMAN] Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal lactosamine unit of a glycoprotein or a glycolipid-linked polylactosamine chains through an alpha-1,3 glycosidic linkage and participates in particular to the Lewis x (Lex)/CD15 epitope biosynthesis in neurons which allows cell differentiation, cell adhesion, and initiation of neurite outgrowth (PubMed:23263199, PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574, PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078, PubMed:16282604, PubMed:29593094). Also fucosylates di-, tri- and tetraantennary N-glycans linked to glycoproteins and the inner lactosamine unit of the alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope synthesis (PubMed:12107078, PubMed:18395013). Furthermore, it is capable of synthesizing Lewis a (Lea), although to a lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex synthesis (PubMed:18395013, PubMed:23192350). May also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE.<ref>PMID:10386598</ref> <ref>PMID:10622713</ref> <ref>PMID:11278338</ref> <ref>PMID:12107078</ref> <ref>PMID:16282604</ref> <ref>PMID:17335083</ref> <ref>PMID:18395013</ref> <ref>PMID:23000574</ref> <ref>PMID:23192350</ref> <ref>PMID:23263199</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Kadirvelraj R]]
+[[Category: Wood ZA]]

8d0x: Difference between revisions

Revision as of 04:03, 25 May 2023

Human FUT9 bound to LNnT

Structural highlights

Function

References

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