1bco: Difference between revisions
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[[Image:1bco.gif|left|200px]] | [[Image:1bco.gif|left|200px]] | ||
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN''' | {{Structure | ||
|PDB= 1bco |SIZE=350|CAPTION= <scene name='initialview01'>1bco</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu]) | |||
}} | |||
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BCO is a [ | 1BCO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration., Rice P, Mizuuchi K, Cell. 1995 Jul 28;82(2):209-20. PMID:[http:// | Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration., Rice P, Mizuuchi K, Cell. 1995 Jul 28;82(2):209-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7628012 7628012] | ||
[[Category: Enterobacteria phage mu]] | [[Category: Enterobacteria phage mu]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: polynucleotidyl transferase]] | [[Category: polynucleotidyl transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:13 2008'' | ||
Revision as of 08:09, 20 March 2008
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| 1bco, resolution 2.4Å | |||||||||||||
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| Gene: | MUA (AMINO ACIDS 248-574) (Enterobacteria phage Mu) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN
Overview
The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4 A resolution. The first of two subdomains contains the active site and, despite very limited sequence homology, exhibits a striking similarity to the core domain of HIV-1 integrase, which carries out a similar set of biochemical reactions. It also exhibits more limited similarity to other nucleases, RNase H and RuvC. The second, a beta barrel, connects to the first subdomain through several contacts. Three independent determinations of the monomer structure from two crystal forms all show the active site held in a similar, apparently inactive configuration. The enzymatic activity of MuA is known to be activated by formation of a DNA-bound tetramer of the protein. We propose that the connections between the two subdomains may be involved in the cross-talk between the active site and the other domains of the transposase that controls the activity of the protein.
About this Structure
1BCO is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration., Rice P, Mizuuchi K, Cell. 1995 Jul 28;82(2):209-20. PMID:7628012
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