1ION

THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3

Summary for 1ION

• Entry DOI: 10.2210/pdb1ion/pdb
• Descriptor: PROBABLE CELL DIVISION INHIBITOR MIND, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: adp-binding protein, p-loop, mind, cell division inhibitor, cell cycle
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 26956.11

Authors

Sakai, N.,Yao, M.,Itou, H.,Watanabe, N.,Yumoto, F.,Tanokura, M.,Tanaka, I. (deposition date: 2001-03-21, release date: 2001-09-26, Last modification date: 2024-11-20)

Primary citation

Sakai, N.,Yao, M.,Itou, H.,Watanabe, N.,Yumoto, F.,Tanokura, M.,Tanaka, I.
The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP.
Structure, 9:817-826, 2001

PubMed Abstract: In Escherichia coli, the cell division site is determined by the cooperative activity of min operon products MinC, MinD, and MinE. MinC is a nonspecific inhibitor of the septum protein FtsZ, and MinE is the supressor of MinC. MinD plays a multifunctional role. It is a membrane-associated ATPase and is a septum site-determining factor through the activation and regulation of MinC and MinE. MinD is also known to undergo a rapid pole-to-pole oscillation movement in vivo as observed by fluorescent microscopy.

PubMed: 11566131
DOI: 10.1016/S0969-2126(01)00638-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)