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==N77Y point mutant of yNTF2 bound to FxFG nucleoporin repeat== | |||
<StructureSection load='1gyb' size='340' side='right'caption='[[1gyb]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gyb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1gyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyb OCA], [https://pdbe.org/1gyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyb RCSB], [https://www.ebi.ac.uk/pdbsum/1gyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NTF2_YEAST NTF2_YEAST] Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. In vitro, the NTF2-Ran-GDP association, in the presence of GTP, triggers dissociation of the karyopherin alpha-beta complex, allowing nuclear translocation of karyopherin alpha and the NLS substrate. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyb_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gyb ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Interactions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 A resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-beta and TAP/p15 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking. | |||
Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats.,Bayliss R, Leung SW, Baker RP, Quimby BB, Corbett AH, Stewart M EMBO J. 2002 Jun 17;21(12):2843-53. PMID:12065398<ref>PMID:12065398</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gyb" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: Bayliss | [[Category: Bayliss R]] | ||
[[Category: Stewart | [[Category: Stewart M]] | ||
Latest revision as of 11:52, 9 May 2024
N77Y point mutant of yNTF2 bound to FxFG nucleoporin repeatN77Y point mutant of yNTF2 bound to FxFG nucleoporin repeat
Structural highlights
FunctionNTF2_YEAST Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import. In vitro, the NTF2-Ran-GDP association, in the presence of GTP, triggers dissociation of the karyopherin alpha-beta complex, allowing nuclear translocation of karyopherin alpha and the NLS substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInteractions with nucleoporins containing FxFG-repeat cores are crucial for the nuclear import of RanGDP mediated by nuclear transport factor 2 (NTF2). We describe here the 1.9 A resolution crystal structure of yeast NTF2-N77Y bound to a FxFG-nucleoporin core, which provides a basis for understanding this interaction and its role in nuclear trafficking. The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2. Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast. Comparison with the crystal structure of FG-nucleoporin cores bound to importin-beta and TAP/p15 identified a number of common features of their binding sites. The structure of the binding interfaces on these transport factors provides a rationale for the specificity of their interactions with nucleoporins that, combined with their weak binding constants, facilitates rapid translocation through NPCs during nuclear trafficking. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats.,Bayliss R, Leung SW, Baker RP, Quimby BB, Corbett AH, Stewart M EMBO J. 2002 Jun 17;21(12):2843-53. PMID:12065398[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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