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| {{STRUCTURE_1g3q| PDB=1g3q | SCENE= }} | | {{STRUCTURE_1g3q| PDB=1g3q | SCENE= }} |
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| '''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''
| | ===CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11296216}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11296216 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11296216}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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 Fri May 2 17:06:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:22:10 2008'' |