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| {{STRUCTURE_2fco| PDB=2fco | SCENE= }} | | {{STRUCTURE_2fco| PDB=2fco | SCENE= }} |
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| '''Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase'''
| | ===Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase=== |
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| ==Overview==
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| Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a "mushroom" like structure with a rigid cap and two highly flexible loops extending outwards. These loops appear to be highly flexible/dynamic, and presumably are directly involved in DNA binding and holding it for catalysis. Structural modifications of both the protein and DNA upon their interaction are essential for catalysis. An Mg2+ ion is present in each of the two active sites in this homodimeric enzyme, and two water molecules are coordinated with each Mg2+ ion. Our data are consistent with one of these water molecules acting as a nucleophile and the other as a general acid. The identities of the general base and general acid involved in catalysis and the Lewis acid that stabilizes the pentacovalent transition state phosphate ion are proposed. A model for the RecU-Holliday junction DNA complex is also proposed and discussed in the context of DNA binding and cleavage.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17557334}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17557334 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17557334}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Flexibility]] | | [[Category: Flexibility]] |
| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:44:20 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:00:41 2008'' |
