1ion

From Proteopedia
Revision as of 23:11, 24 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1ion" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ion, resolution 2.30Å" /> '''THE SEPTUM SITE-DETE...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1ion.gif


1ion, resolution 2.30Å

Drag the structure with the mouse to rotate

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

OverviewOverview

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 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. RESULTS: The three-dimensional structure of the, MinD-2 from Pyrococcus horikoshii OT3 (PH0612) has been determined at 2.3, A 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 bound ADP 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 monomer in, the crystal. Both the 31P 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.

About this StructureAbout this Structure

1ION is a Single protein structure of sequence from Pyrococcus horikoshii with MG and ADP as ligands. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP., Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I, Structure. 2001 Sep;9(9):817-26. PMID:11566131

Page seeded by OCA on Sat Nov 24 22:18:38 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA