1G3Q

CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND

Summary for 1G3Q

• Entry DOI: 10.2210/pdb1g3q/pdb
• Descriptor: CELL DIVISION INHIBITOR, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: alpha-beta-alpha layered, protein-adp complex, cell cycle, hydrolase
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 25786.85

Authors

Hayashi, I.,Oyama, T.,Morikawa, K. (deposition date: 2000-10-25, release date: 2001-04-21, Last modification date: 2024-02-07)

Primary citation

Hayashi, I.,Oyama, T.,Morikawa, K.
Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.
EMBO J., 20:1819-1828, 2001

PubMed Abstract: Proper placement of the bacterial cell division site requires the site-specific inactivation of other potential division sites. In Escherichia coli, selection of the correct mid-cell site is mediated by the MinC, MinD and MinE proteins. To clarify the functional role of the bacterial cell division inhibitor MinD, which is a membrane-associated ATPase that works as an activator of MinC, we determined the crystal structure of a Pyrococcus furiosus MinD homologue complexed with a substrate analogue, AMPPCP, and with the product ADP at resolutions of 2.7 and 2.0 A, respectively. The structure reveals general similarities to the nitrogenase iron protein, the H-Ras p21 and the RecA-like ATPase domain. Alanine scanning mutational analyses of E.coli MinD were also performed in vivo. The results suggest that the residues around the ATP-binding site are required for the direct interaction with MinC, and that ATP binding and hydrolysis play a role as a molecular switch to control the mechanisms of MinCDE-dependent bacterial cell division.

PubMed: 11296216
DOI: 10.1093/emboj/20.8.1819

Experimental method

X-RAY DIFFRACTION (2 Å)