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2efk
From Proteopedia
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| - | [[Image:2efk.jpg|left|200px]]<br /><applet load="2efk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2efk, resolution 2.30Å" /> | ||
| - | '''Crystal structure of the EFC domain of Cdc42-interacting protein 4'''<br /> | ||
| - | == | + | ==Crystal structure of the EFC domain of Cdc42-interacting protein 4== |
| + | <StructureSection load='2efk' size='340' side='right'caption='[[2efk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2efk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFK FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efk OCA], [https://pdbe.org/2efk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efk RCSB], [https://www.ebi.ac.uk/pdbsum/2efk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efk ProSAT], [https://www.topsan.org/Proteins/RSGI/2efk TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CIP4_HUMAN CIP4_HUMAN]] Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:11069762</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</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/ef/2efk_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=2efk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role. | Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role. | ||
| - | + | Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.,Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S Cell. 2007 May 18;129(4):761-72. PMID:17512409<ref>PMID:17512409</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2efk" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Chen, L | + | <references/> |
| - | [[Category: Liu, Z J | + | __TOC__ |
| - | [[Category: Niwa, H | + | </StructureSection> |
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: Shimada, A | + | [[Category: Large Structures]] |
| - | [[Category: Shirouzu, M | + | [[Category: Chen, L]] |
| - | [[Category: Terada, T | + | [[Category: Liu, Z J]] |
| - | [[Category: Wang, B C | + | [[Category: Niwa, H]] |
| - | [[Category: Yokoyama, S | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Shimada, A]] |
| - | [[Category: | + | [[Category: Shirouzu, M]] |
| - | [[Category: | + | [[Category: Terada, T]] |
| - | + | [[Category: Wang, B C]] | |
| - | [[Category: | + | [[Category: Yokoyama, S]] |
| - | [[Category: | + | [[Category: Efc domain]] |
| - | + | [[Category: Endocytosis-exocytosis complex]] | |
| - | + | [[Category: National project on protein structural and functional analyse]] | |
| + | [[Category: Nppsfa]] | ||
| + | [[Category: Rsgi]] | ||
Current revision
Crystal structure of the EFC domain of Cdc42-interacting protein 4
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