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1g3r

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[[Image:1g3r.gif|left|200px]]<br /><applet load="1g3r" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g3r.gif|left|200px]]
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caption="1g3r, resolution 2.70&Aring;" />
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'''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''<br />
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{{Structure
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|PDB= 1g3r |SIZE=350|CAPTION= <scene name='initialview01'>1g3r</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'>ACP</scene>
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|ACTIVITY=
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|GENE= MIND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])
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}}
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'''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1G3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ACP:'>ACP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3R OCA].
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1G3R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3R OCA].
==Reference==
==Reference==
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Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus., Hayashi I, Oyama T, Morikawa K, EMBO J. 2001 Apr 17;20(8):1819-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11296216 11296216]
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Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus., Hayashi I, Oyama T, Morikawa K, EMBO J. 2001 Apr 17;20(8):1819-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11296216 11296216]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein-adp complex]]
[[Category: protein-adp complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:17:46 2008''

Revision as of 09:17, 20 March 2008


PDB ID 1g3r

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: and
Gene: MIND (Pyrococcus furiosus)
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND


Overview

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.

About this Structure

1G3R is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus., Hayashi I, Oyama T, Morikawa K, EMBO J. 2001 Apr 17;20(8):1819-28. PMID:11296216

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