Publikationsdatum:
2012-03-09
Beschreibung:
Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 A resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kon, Takahide -- Oyama, Takuji -- Shimo-Kon, Rieko -- Imamula, Kenji -- Shima, Tomohiro -- Sutoh, Kazuo -- Kurisu, Genji -- England -- Nature. 2012 Mar 7;484(7394):345-50. doi: 10.1038/nature10955.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. takahide.kon@protein.osaka-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22398446" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Adenosine Diphosphate/metabolism
;
Adenosine Triphosphate/metabolism
;
Allosteric Regulation
;
Binding Sites
;
Crystallography, X-Ray
;
Cytoplasmic Dyneins/*chemistry/metabolism
;
Dictyostelium/*chemistry
;
Hydrolysis
;
Microtubules/metabolism
;
Models, Biological
;
Models, Molecular
;
Movement
;
Protein Structure, Tertiary
;
Structure-Activity Relationship
Print ISSN:
0028-0836
Digitale ISSN:
1476-4687
Thema:
Biologie
,
Chemie und Pharmazie
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
Permalink
