5FM6

Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(apo)

Summary for 5FM6

• Entry DOI: 10.2210/pdb5fm6/pdb
• Related: 5FLV 5FM7
• Descriptor: RVB1, RVB2, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: unknown function, rvb1, rvb2, adp, atp binding protein
• Biological source: CHAETOMIUM THERMOPHILUM; More
• Total number of polymer chains: 2
• Total formula weight: 105757.26

Authors

Silva-Martin, N.,Dauden, M.I.,Glatt, S.,Hoffmann, N.A.,Mueller, C.W. (deposition date: 2015-11-02, release date: 2016-01-20, Last modification date: 2024-10-23)

Primary citation

Silva-Martin, N.,Dauden, M.I.,Glatt, S.,Hoffmann, N.A.,Kastritis, P.,Bork, P.,Beck, M.,Muller, C.W.
The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight Into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.
Plos One, 11:46457-, 2016

PubMed Abstract: The Rvb1/Rvb2 complex is an essential component of many cellular pathways. The Rvb1/Rvb2 complex forms a dodecameric assembly where six copies of each subunit form two heterohexameric rings. However, due to conformational variability, the way the two rings pack together is still not fully understood. Here, we present the crystal structure and two cryo-electron microscopy reconstructions of the dodecameric, full-length Rvb1/Rvb2 complex, all showing that the interaction between the two heterohexameric rings is mediated through the Rvb1/Rvb2-specific domain II. Two conformations of the Rvb1/Rvb2 dodecamer are present in solution: a stretched conformation also present in the crystal, and a compact conformation. Novel asymmetric features observed in the reconstruction of the compact conformation provide additional insight into the plasticity of the Rvb1/Rvb2 complex.

PubMed: 26745716
DOI: 10.1371/JOURNAL.PONE.0146457

Experimental method

X-RAY DIFFRACTION (2.997 Å)