de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Three−dimensional structure of the complex of actin and DNase I at 4.5 A resolution

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons93650

Kabsch,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94211

Mannherz,  Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Kabsch, W., Mannherz, H. G., & Suck, D. (1985). Three−dimensional structure of the complex of actin and DNase I at 4.5 A resolution. EMBO Journal, 4(8), 2113-2118. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd%3DRetrieve%26db%3DPubMed%26list_uids%3D4065103%26dopt%3DAbstract.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AF57-5
Abstract
The shape of an actin subunit has been derived from an improved 6 A map of the complex of rabbit skeletal muscle actin and bovine pancreatic DNase I obtained by X−ray crystallographic methods. The three−dimensional structure of DNase I determined independently at 2.5 A resolution was compared with the DNase I electron density in the actin:DNase map. The two structures are very similar at 6 A resolution thus leading to an unambiguous identification of actin as well as DNase I electron density. Furthermore the correct hand of the actin structure is determined from the DNase I atomic structure. The resolution of the actin structure was extended to 4.5 A by using a single heavy−atom derivative and the knowledge of the atomic coordinates of DNase I. The dimensions of an actin subunit are 67 A X 40 A X 37 A. It consists of a small and a large domain, the small domain containing the N terminus. Actin is an alpha,beta−protein with a beta−pleated sheet in each domain. These sheets are surrounded by several alpha−helices, comprising at least 40% of the structure. The phosphate peak of the adenine nucleotide is located between the two domains. The complex of actin and DNase I as found in solution (i.e., the actin:DNase I contacts which do not depend on crystal packing) was deduced from a comparison of monoclinic with orthorhombic crystals. Residues 44−46, 51, 52, 60−62 of DNase I are close to a loop region in the small domain of actin. At a distance of approximately 15 A there is a second contact in the large domain in which Glu13 of DNase I is involved. A possible binding region for myosin is discussed