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2l1a

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Revision as of 07:34, 14 April 2021

Solution NMR structure of the N-terminal GTPase-like domain of dictyostelium discoideum Fomin C

Structural highlights

2l1a is a 1 chain structure with sequence from Atcc 11735. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	forC, DDB_G0287295 (ATCC 11735)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FORC_DICDI] Formins play an important role in the nucleation of actin and the formation of linear actin filaments.^[1]

Publication Abstract from PubMed

Dictyostelium Formin C (ForC) is involved in the regulation of local actin cytoskeleton reorganization (e.g. during cellular adhesion or migration). ForC contains formin homology 2 and 3 (FH2 and -3) domains and an N-terminal putative GTPase-binding domain (GBD) but lacks a canonical FH1 region. To better understand the role of the GBD, its structure, dynamics, lipid-binding properties, and cellular functions were analyzed by NMR and CD spectroscopy and by in vivo fluorescence microscopy. Moreover, the program CS-Rosetta was tested for the structure prediction based on chemical shift data only. The ForC GBD adopts an ubiquitin-like alpha/beta-roll fold with an unusually long loop between beta-strands 1 and 2. Based on the lipid-binding data, the presence of DPC micelles induces the formation of alpha-helical secondary structure and a rearrangement of the tertiary structure. Lipid-binding studies with a mutant protein and a peptide suggest that the beta1-beta2 loop is not relevant for these conformational changes. Whereas small amounts of negatively charged phosphoinositides (1,2-dioctanoyl-sn-glycero-3-(phosphoinositol 4,5-bisphosphate) and 1,2-dihexanoyl-sn-glycero-3-(phosphoinositol 3,4,5-trisphosphate)) lower the micelle concentration necessary to induce the observed spectral changes, other negatively charged phospholipids (1,2-dihexanoyl-sn-glycero-3-(phospho-L-serine) and 1,2-dihexanoyl-sn-glycero-3-phospho-(1'-rac-glycerol)) had no such effect. Interestingly, bicelles and micelles composed of diacylphosphocholines had no effect on the GBD structure. Our data suggest a model in which part of the large positively charged surface area of the GBD mediates localization to specific membrane patches, thereby regulating interactions with signaling proteins. Our cellular localization studies show that both the GBD and the FH3 domain are required for ForC targeting to cell-cell contacts and early phagocytic cups and macropinosomes.

Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C.,Dames SA, Junemann A, Sass HJ, Schonichen A, Stopschinski BE, Grzesiek S, Faix J, Geyer M J Biol Chem. 2011 Oct 21;286(42):36907-20. doi: 10.1074/jbc.M111.225052. Epub, 2011 Aug 16. PMID:21846933^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kitayama C, Uyeda TQ. ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum. J Cell Sci. 2003 Feb 15;116(Pt 4):711-23. PMID:12538772
↑ Dames SA, Junemann A, Sass HJ, Schonichen A, Stopschinski BE, Grzesiek S, Faix J, Geyer M. Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C. J Biol Chem. 2011 Oct 21;286(42):36907-20. doi: 10.1074/jbc.M111.225052. Epub, 2011 Aug 16. PMID:21846933 doi:http://dx.doi.org/10.1074/jbc.M111.225052

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l1a"

@@ Line 1: / Line 1: @@
 ==Solution NMR structure of the N-terminal GTPase-like domain of dictyostelium discoideum Fomin C==
-<StructureSection load='2l1a' size='340' side='right' caption='[[2l1a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l1a' size='340' side='right'caption='[[2l1a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l1a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L1A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l1a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L1A FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">forC, DDB_G0287295 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">forC, DDB_G0287295 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</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=2l1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1a OCA], [http://pdbe.org/2l1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l1a RCSB], [http://www.ebi.ac.uk/pdbsum/2l1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l1a 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=2l1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1a OCA], [https://pdbe.org/2l1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l1a RCSB], [https://www.ebi.ac.uk/pdbsum/2l1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l1a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FORC_DICDI FORC_DICDI]] Formins play an important role in the nucleation of actin and the formation of linear actin filaments.<ref>PMID:12538772</ref>
+[[https://www.uniprot.org/uniprot/FORC_DICDI FORC_DICDI]] Formins play an important role in the nucleation of actin and the formation of linear actin filaments.<ref>PMID:12538772</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[Category: Atcc 11735]]
+[[Category: Large Structures]]
 [[Category: Dames, S A]]
 [[Category: Geyer, M]]

2l1a

From Proteopedia

Revision as of 07:34, 14 April 2021

Solution NMR structure of the N-terminal GTPase-like domain of dictyostelium discoideum Fomin C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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