3nd2: Difference between revisions
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< | ==Structure of Yeast Importin-beta (Kap95p)== | ||
<StructureSection load='3nd2' size='340' side='right'caption='[[3nd2]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ND2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ND2 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]] 2.4Å</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=3nd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nd2 OCA], [https://pdbe.org/3nd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3nd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nd2 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IMB1_YEAST IMB1_YEAST] Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.<ref>PMID:11309407</ref> | |||
== 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/nd/3nd2_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=3nd2 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways. | |||
Quantitative structural analysis of importin-beta flexibility: paradigm for solenoid protein structures.,Forwood JK, Lange A, Zachariae U, Marfori M, Preast C, Grubmuller H, Stewart M, Corbett AH, Kobe B Structure. 2010 Sep 8;18(9):1171-83. PMID:20826343<ref>PMID:20826343</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3nd2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Importin 3D structures|Importin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | |||
== | |||
< | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Forwood | [[Category: Forwood JK]] | ||
[[Category: Kobe | [[Category: Kobe B]] | ||
Latest revision as of 19:45, 1 November 2023
Structure of Yeast Importin-beta (Kap95p)Structure of Yeast Importin-beta (Kap95p)
Structural highlights
FunctionIMB1_YEAST Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Serves a receptor for nuclear localization signals. Mediates the nuclear import of histones H2A and H2B.[1] 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 PubMedThe structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-beta, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-beta flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-beta (Kap95) to allow a quantitative comparison with importin-beta bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-beta illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways. Quantitative structural analysis of importin-beta flexibility: paradigm for solenoid protein structures.,Forwood JK, Lange A, Zachariae U, Marfori M, Preast C, Grubmuller H, Stewart M, Corbett AH, Kobe B Structure. 2010 Sep 8;18(9):1171-83. PMID:20826343[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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