3g9g: Difference between revisions

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<StructureSection load='3g9g' size='340' side='right'caption='[[3g9g]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3g9g' size='340' side='right'caption='[[3g9g]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3g9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9G FirstGlance]. <br>
<table><tr><td colspan='2'>[[3g9g]] 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=3G9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9G FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3g9h|3g9h]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYP1, YCR030C, YCR30C/YCR29C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3g9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9g OCA], [https://pdbe.org/3g9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9g RCSB], [https://www.ebi.ac.uk/pdbsum/3g9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9g ProSAT]</span></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=3g9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9g OCA], [https://pdbe.org/3g9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9g RCSB], [https://www.ebi.ac.uk/pdbsum/3g9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SYP1_YEAST SYP1_YEAST]] Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.<ref>PMID:11014808</ref> <ref>PMID:18791237</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref>
[https://www.uniprot.org/uniprot/SYP1_YEAST SYP1_YEAST] Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.<ref>PMID:11014808</ref> <ref>PMID:18791237</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3g9g ConSurf].
</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=3g9g ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding mu homology domains (muHDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The muHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.
Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.,Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939<ref>PMID:19713939</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3g9g" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barker, S]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hurley, J]]
[[Category: Barker S]]
[[Category: Im, Y J]]
[[Category: Hurley J]]
[[Category: Maldonado-Baez, L]]
[[Category: Im YJ]]
[[Category: Mishra, S]]
[[Category: Maldonado-Baez L]]
[[Category: Reider, A]]
[[Category: Mishra S]]
[[Category: Traub, L]]
[[Category: Reider A]]
[[Category: Wendland, B]]
[[Category: Traub L]]
[[Category: Adaptor]]
[[Category: Wendland B]]
[[Category: Bar domain]]
[[Category: Endocytosis]]
[[Category: Fch]]
[[Category: Phosphoprotein]]
[[Category: Syp1]]

Latest revision as of 09:53, 21 February 2024

Crystal Structure of the N-terminal EFC/F-BAR domain of Syp1

3g9g, resolution 2.40Å

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