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1io0

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CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF

Structural highlights

1io0 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9DEA6_CHICK

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 PubMed

Tropomodulin is the unique pointed-end capping protein of the actin-tropomyosin filament. By blocking elongation and depolymerization, tropomodulin regulates the architecture and the dynamics of the filament. Here we report the crystal structure at 1.45-A resolution of the C-terminal half of tropomodulin (C20), the actin-binding moiety of tropomodulin. C20 is a leucine-rich repeat domain, and this is the first actin-associated protein with a leucine-rich repeat. Binding assays suggested that C20 also interacts with the N-terminal fragment, M1-M2-M3, of nebulin. Based on the crystal structure, we propose a model for C20 docking to the actin subunit at the pointed end. Although speculative, the model is consistent with the idea that a tropomodulin molecule competes with an actin subunit for a pointed end. The model also suggests that interactions with tropomyosin, actin, and nebulin are all possible sources of influences on the dynamic properties of pointed-end capping by tropomodulin.

Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping.,Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704^[1]

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

References

↑ Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y. Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1io0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1io0' size='340' side='right'caption='[[1io0]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1io0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IO0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1io0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.45&#8491;</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=1io0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io0 OCA], [http://pdbe.org/1io0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1io0 RCSB], [http://www.ebi.ac.uk/pdbsum/1io0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1io0 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1io0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io0 OCA], [https://pdbe.org/1io0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io0 RCSB], [https://www.ebi.ac.uk/pdbsum/1io0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9DEA6_CHICK Q9DEA6_CHICK]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Kostyukova, A]]
+[[Category: Kostyukova A]]
-[[Category: Krieger, I]]
+[[Category: Krieger I]]
-[[Category: Maeda, Y]]
+[[Category: Maeda Y]]
-[[Category: Yamashita, A]]
+[[Category: Yamashita A]]
-[[Category: Lrr protein]]
-[[Category: Protein binding]]
-[[Category: Right-handed super-helix]]

1io0

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Current revision

CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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