2zwh

From Proteopedia

(Difference between revisions)

Current revision

Model for the F-actin structure

Structural highlights

2zwh is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Fiber diffraction, Resolution 3.3Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Publication Abstract from PubMed

Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.

The nature of the globular- to fibrous-actin transition.,Oda T, Iwasa M, Aihara T, Maeda Y, Narita A Nature. 2009 Jan 22;457(7228):441-5. PMID:19158791^[1]

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

References

↑ Oda T, Iwasa M, Aihara T, Maeda Y, Narita A. The nature of the globular- to fibrous-actin transition. Nature. 2009 Jan 22;457(7228):441-5. PMID:19158791 doi:10.1038/nature07685

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2zwh' size='340' side='right'caption='[[2zwh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2zwh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zwh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZWH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Fiber diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=2zwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zwh OCA], [https://pdbe.org/2zwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zwh RCSB], [https://www.ebi.ac.uk/pdbsum/2zwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zwh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
+[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: European rabbit]]
 [[Category: Large Structures]]
-[[Category: Aihara, T]]
+[[Category: Oryctolagus cuniculus]]
-[[Category: Iwasa, M]]
+[[Category: Aihara T]]
-[[Category: Maeda, Y]]
+[[Category: Iwasa M]]
-[[Category: Narita, A]]
+[[Category: Maeda Y]]
-[[Category: Oda, T]]
+[[Category: Narita A]]
-[[Category: Atp-binding]]
+[[Category: Oda T]]
-[[Category: Contractile protein]]
-[[Category: Cytoskeleton]]
-[[Category: Cytoskelton]]
-[[Category: F-actin]]
-[[Category: G-actin]]
-[[Category: Methylation]]
-[[Category: Muscle protein]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]

2zwh

From Proteopedia

Current revision

Model for the F-actin structure

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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