2XVC

Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division

Summary for 2XVC

• Entry DOI: 10.2210/pdb2xvc/pdb
• Descriptor: ESCRT-III, CDVA, SSO0911, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: cell cycle, cell division, cytokinesis, winged-helix
• Biological source: SULFOLOBUS SOLFATARICUS; More
• Total number of polymer chains: 2
• Total formula weight: 8690.66

Authors

Samson, R.Y.,Obita, T.,Hodgson, B.,Shaw, M.K.,Chong, P.L.,Williams, R.L.,Bell, S.D. (deposition date: 2010-10-25, release date: 2011-02-02, Last modification date: 2024-05-08)

Primary citation

Samson, R.Y.,Obita, T.,Hodgson, B.,Shaw, M.K.,Chong, P.L.,Williams, R.L.,Bell, S.D.
Molecular and Structural Basis of Escrt-III Recruitment to Membranes During Archaeal Cell Division.
Mol.Cell, 41:186-, 2011

PubMed Abstract: Members of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESCRT machinery play an important role in Sulfolobus cell division. In eukaryotes, several pathways recruit ESCRT-III proteins to their sites of action. However, the positioning determinants for archaeal ESCRT-III are not known. Here, we identify a protein, CdvA, that is responsible for recruiting Sulfolobus ESCRT-III to membranes. Overexpression of the isolated ESCRT-III domain that interacts with CdvA results in the generation of nucleoid-free cells. Furthermore, CdvA and ESCRT-III synergize to deform archaeal membranes in vitro. The structure of the CdvA/ESCRT-III interface gives insight into the evolution of the more complex and modular eukaryotic ESCRT complex.

PubMed: 21255729
DOI: 10.1016/J.MOLCEL.2010.12.018

Experimental method

X-RAY DIFFRACTION (2.15 Å)