5jlh

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution

5jlh, resolution 3.90Å

Structural highlights

5jlh is a 11 chain structure with sequence from Dictyostelium discoideum and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.9Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACTG_HUMAN Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

ACTG_HUMAN 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

The interaction of myosin with actin filaments is the central feature of muscle contraction and cargo movement along actin filaments of the cytoskeleton. The energy for these movements is generated during a complex mechanochemical reaction cycle. Crystal structures of myosin in different states have provided important structural insights into the myosin motor cycle when myosin is detached from F-actin. The difficulty of obtaining diffracting crystals, however, has prevented structure determination by crystallography of actomyosin complexes. Thus, although structural models exist of F-actin in complex with various myosins, a high-resolution structure of the F-actin-myosin complex is missing. Here, using electron cryomicroscopy, we present the structure of a human rigor actomyosin complex at an average resolution of 3.9 A. The structure reveals details of the actomyosin interface, which is mainly stabilized by hydrophobic interactions. The negatively charged amino (N) terminus of actin interacts with a conserved basic motif in loop 2 of myosin, promoting cleft closure in myosin. Surprisingly, the overall structure of myosin is similar to rigor-like myosin structures in the absence of F-actin, indicating that F-actin binding induces only minimal conformational changes in myosin. A comparison with pre-powerstroke and intermediate (Pi-release) states of myosin allows us to discuss the general mechanism of myosin binding to F-actin. Our results serve as a strong foundation for the molecular understanding of cytoskeletal diseases, such as autosomal dominant hearing loss and diseases affecting skeletal and cardiac muscles, in particular nemaline myopathy and hypertrophic cardiomyopathy.

Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution.,von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ, Raunser S Nature. 2016 Jun 30;534(7609):724-8. PMID:27324845^[1]

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

References

↑ von der Ecken J, Heissler SM, Pathan-Chhatbar S, Manstein DJ, Raunser S. Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution. Nature. 2016 Jun 30;534(7609):724-8. PMID:27324845 doi:http://dx.doi.org/10.1038/nature18295

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jlh"

@@ Line 3: / Line 3: @@
 <SX load='5jlh' size='340' side='right' viewer='molstar' caption='[[5jlh]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jlh]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JLH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jlh]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JLH 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTG1, ACTG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), abpA, actnA, DDB_G0268632 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5jlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlh OCA], [https://pdbe.org/5jlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jlh RCSB], [https://www.ebi.ac.uk/pdbsum/5jlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jlh ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlh OCA], [http://pdbe.org/5jlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jlh RCSB], [http://www.ebi.ac.uk/pdbsum/5jlh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jlh ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN]] Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/MYH14_HUMAN MYH14_HUMAN]] Peripheral neuropathy-myopathy-hoarseness-hearing loss syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/MYH14_HUMAN MYH14_HUMAN]] Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
+[https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] 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 25: @@
 *[[Actin 3D structures|Actin 3D structures]]
 *[[Actinin 3D structures|Actinin 3D structures]]
-*[[Tropomyosin|Tropomyosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Human]]
+[[Category: Dictyostelium discoideum]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ecken, J von der]]
+[[Category: Heissler SM]]
-[[Category: Heissler, S M]]
+[[Category: Manstein DJ]]
-[[Category: Manstein, D J]]
+[[Category: Pathan-Chhatbar S]]
-[[Category: Pathan-Chhatbar, S]]
+[[Category: Raunser S]]
-[[Category: Raunser, S]]
+[[Category: Von der Ecken J]]
-[[Category: Contractile filament]]
-[[Category: Contractile protein]]
-[[Category: Cryo em]]
-[[Category: Cytoskeleton]]
-[[Category: F-actin]]
-[[Category: Filament]]
-[[Category: Hydrolase complex]]
-[[Category: Muscle]]
-[[Category: Myosin]]
-[[Category: Protein polymer]]
-[[Category: Structural protein]]
-[[Category: Thin filament]]
-[[Category: Tropomyosin]]

5jlh

From Proteopedia

Current revision

Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox