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1g3q
From Proteopedia
(New page: 200px<br /><applet load="1g3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g3q, resolution 2.00Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1g3q.gif|left|200px]]<br /><applet load="1g3q" size=" | + | [[Image:1g3q.gif|left|200px]]<br /><applet load="1g3q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g3q, resolution 2.00Å" /> | caption="1g3q, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proper placement of the bacterial cell division site requires the | + | 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== | ==About this Structure== | ||
| - | 1G3Q 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:// | + | 1G3Q 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== | ==Reference== | ||
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[[Category: protein-adp complex]] | [[Category: protein-adp complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:46 2008'' |
Revision as of 10:45, 21 February 2008
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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
1G3Q is a Single protein structure of sequence from Pyrococcus furiosus with and as ligands. 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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