1bcm

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(New page: 200px<br /><applet load="1bcm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bcm, resolution 2.8&Aring;" /> '''BACTERIOPHAGE MU TRAN...)
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[[Image:1bcm.gif|left|200px]]<br /><applet load="1bcm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bcm, resolution 2.8&Aring;" />
caption="1bcm, resolution 2.8&Aring;" />
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT'''<br />
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT'''<br />
==Overview==
==Overview==
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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.
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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==
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1BCM 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BCM OCA].
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1BCM 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=1BCM OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mizuuchi, K.]]
[[Category: Mizuuchi, K.]]
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[[Category: Rice, P.A.]]
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[[Category: Rice, P A.]]
[[Category: dna binding]]
[[Category: dna binding]]
[[Category: endonuclease]]
[[Category: endonuclease]]
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[[Category: polynucleotidyl transferase]]
[[Category: polynucleotidyl transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:32:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:50 2008''

Revision as of 09:53, 21 February 2008


1bcm, resolution 2.8Å

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BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT

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

1BCM 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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