1g3q: Difference between revisions

Revision as of 13:45, 21 February 2008

CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND

OverviewOverview

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 StructureAbout this Structure

1G3Q is a Single protein structure of sequence from Pyrococcus furiosus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:45:46 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1g3q.gif|left|200px]]<br /><applet load="1g3q" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g3q.gif|left|200px]]<br /><applet load="1g3q" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g3q, resolution 2.00&Aring;" />
 '''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''<br />
 ==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.
+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==
-G3Q 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 MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G3Q OCA].
+G3Q 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=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3Q OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: protein-adp complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:47:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:46 2008''