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1g3r
From Proteopedia
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|PDB= 1g3r |SIZE=350|CAPTION= <scene name='initialview01'>1g3r</scene>, resolution 2.70Å | |PDB= 1g3r |SIZE=350|CAPTION= <scene name='initialview01'>1g3r</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MIND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | |GENE= MIND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3r OCA], [http://www.ebi.ac.uk/pdbsum/1g3r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g3r RCSB]</span> | ||
}} | }} | ||
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[[Category: Morikawa, K.]] | [[Category: Morikawa, K.]] | ||
[[Category: Oyama, T.]] | [[Category: Oyama, T.]] | ||
| - | [[Category: ACP]] | ||
| - | [[Category: MG]] | ||
[[Category: alpha-beta-alpha layered]] | [[Category: alpha-beta-alpha layered]] | ||
[[Category: protein-adp complex]] | [[Category: protein-adp complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:35:57 2008'' |
Revision as of 17:35, 30 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | MIND (Pyrococcus furiosus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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