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Titolo:
The three-dimensional structure of septum site- determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP
Autore:
Sakai, N; Yao, M; Itou, H; Watanabe, N; Yumoto, F; Tanokura, M; Tanaka, I;
Indirizzi:
Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 oro, Hokkaido 0600810, Japan Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 Dept Appl Biol Chem, Tokyo 1138657, Japan
Titolo Testata:
STRUCTURE
fascicolo: 9, volume: 9, anno: 2001,
pagine: 817 - 826
SICI:
0969-2126(200109)9:9<817:TTSOSS>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; TOPOLOGICAL SPECIFICITY FACTOR; DIVISION INHIBITOR MINC; BACTERIAL-CELL DIVISION; TO-POLE OSCILLATION; ESCHERICHIA-COLI; MYOSIN SUBFRAGMENT-1; ADENOSINE-DIPHOSPHATE; PROPER PLACEMENT; RAPID POLE;
Keywords:
ATPase; cell division; MinD; motor protein; x-ray structure; MAD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Tanaka, I Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 ido 0600810, Japan
Citazione:
N. Sakai et al., "The three-dimensional structure of septum site- determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP", STRUCTURE, 9(9), 2001, pp. 817-826

Abstract

Background: 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 andregulation of MinC and MinE. MinD is also known to undergo a rapid pole-to-pole oscillation movement in vivo as observed by fluorescent microscopy. Results: The three-dimensional structure of the MinD-2 from Pyrococcus horikoshii OT3 (PH0612) has been determined at 2.3 Angstrom resolution by X-ray crystallography using the Se-Met MAD method. The molecule consists of a beta sheet with 7 parallel and 1 antiparallel strands and 11 peripheral alpha helices. It contains the classical mononucleotide binding loop with boundADP and magnesium ion, which is consistent with the suggested ATPase activity. Conclusions: Structure analysis shows that MinD is most similar to nitrogenase iron protein, which is a member of the P loop-containing nucleotide triphosphate hydrolase superfamily of proteins. Unlike nitrogenase or other member proteins that normally work as a dimer, MinD was present as a monomerin the crystal. Both the P-31 NMR and Malachite Green method exhibited relatively low levels of ATPase activity. These facts suggest that MinD may work as a molecular switch in the multiprotein complex in bacterial cell division.

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Documento generato il 08/07/20 alle ore 07:44:32