1bco
From Proteopedia
(New page: 200px<br /><applet load="1bco" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bco, resolution 2.4Å" /> '''BACTERIOPHAGE MU TRAN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bco.gif|left|200px]]<br /><applet load="1bco" size=" | + | [[Image:1bco.gif|left|200px]]<br /><applet load="1bco" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bco, resolution 2.4Å" /> | caption="1bco, resolution 2.4Å" /> | ||
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN'''<br /> | '''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN'''<br /> | ||
==Overview== | ==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 | + | 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== | ==About this Structure== | ||
| - | 1BCO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http:// | + | 1BCO is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mizuuchi, K.]] | [[Category: Mizuuchi, K.]] | ||
| - | [[Category: Rice, P | + | [[Category: Rice, P A.]] |
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
| Line 20: | Line 20: | ||
[[Category: polynucleotidyl transferase]] | [[Category: polynucleotidyl transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:57 2008'' |
Revision as of 09:53, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 11:53:57 2008
