6ia7: Difference between revisions
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<StructureSection load='6ia7' size='340' side='right'caption='[[6ia7]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6ia7' size='340' side='right'caption='[[6ia7]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ia7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IA7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ia7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tryb2 Tryb2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IA7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFT22, Tb11.01.8590 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=185431 TRYB2])</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=6ia7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ia7 OCA], [http://pdbe.org/6ia7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ia7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ia7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ia7 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=6ia7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ia7 OCA], [http://pdbe.org/6ia7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ia7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ia7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ia7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/IFT22_TRYB2 IFT22_TRYB2]] Required for flagellum formation.<ref>PMID:19240117</ref> | [[http://www.uniprot.org/uniprot/IFT22_TRYB2 IFT22_TRYB2]] Required for flagellum formation.<ref>PMID:19240117</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Intraflagellar transport (IFT) relies on motor proteins and the IFT complex to construct cilia and flagella. The IFT complex subunit IFT22/RabL5 has sequence similarity with small GTPases although the nucleotide specificity is unclear because of non-conserved G4/G5 motifs. We show that IFT22 specifically associates with G-nucleotides and present crystal structures of IFT22 in complex with GDP, GTP, and with IFT74/81. Our structural analysis unravels an unusual GTP/GDP-binding mode of IFT22 bypassing the classical G4 motif. The GTPase switch regions of IFT22 become ordered upon complex formation with IFT74/81 and mediate most of the IFT22-74/81 interactions. Structure-based mutagenesis reveals that association of IFT22 with the IFT complex is essential for flagellum construction in Trypanosoma brucei although IFT22 GTP-loading is not strictly required. | |||
Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly.,Wachter S, Jung J, Shafiq S, Basquin J, Fort C, Bastin P, Lorentzen E EMBO J. 2019 Apr 2. pii: embj.2018101251. doi: 10.15252/embj.2018101251. PMID:30940671<ref>PMID:30940671</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ia7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Tryb2]] | |||
[[Category: Basquin, J]] | [[Category: Basquin, J]] | ||
[[Category: Lorentzen, E]] | [[Category: Lorentzen, E]] | ||
Latest revision as of 09:54, 17 April 2019
T. brucei IFT22 GTP-bound crystal structureT. brucei IFT22 GTP-bound crystal structure
Structural highlights
Function[IFT22_TRYB2] Required for flagellum formation.[1] Publication Abstract from PubMedIntraflagellar transport (IFT) relies on motor proteins and the IFT complex to construct cilia and flagella. The IFT complex subunit IFT22/RabL5 has sequence similarity with small GTPases although the nucleotide specificity is unclear because of non-conserved G4/G5 motifs. We show that IFT22 specifically associates with G-nucleotides and present crystal structures of IFT22 in complex with GDP, GTP, and with IFT74/81. Our structural analysis unravels an unusual GTP/GDP-binding mode of IFT22 bypassing the classical G4 motif. The GTPase switch regions of IFT22 become ordered upon complex formation with IFT74/81 and mediate most of the IFT22-74/81 interactions. Structure-based mutagenesis reveals that association of IFT22 with the IFT complex is essential for flagellum construction in Trypanosoma brucei although IFT22 GTP-loading is not strictly required. Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly.,Wachter S, Jung J, Shafiq S, Basquin J, Fort C, Bastin P, Lorentzen E EMBO J. 2019 Apr 2. pii: embj.2018101251. doi: 10.15252/embj.2018101251. PMID:30940671[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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