1bcm

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[[Image:1bcm.gif|left|200px]]
[[Image:1bcm.gif|left|200px]]
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{{Structure
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|PDB= 1bcm |SIZE=350|CAPTION= <scene name='initialview01'>1bcm</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1bcm", creates the "Structure Box" on the page.
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|SITE=
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|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])
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|DOMAIN=
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{{STRUCTURE_1bcm| PDB=1bcm | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcm OCA], [http://www.ebi.ac.uk/pdbsum/1bcm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bcm RCSB]</span>
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'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT'''
'''BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT'''
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[[Category: Mizuuchi, K.]]
[[Category: Mizuuchi, K.]]
[[Category: Rice, P A.]]
[[Category: Rice, P A.]]
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[[Category: dna binding]]
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[[Category: Dna binding]]
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[[Category: endonuclease]]
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[[Category: Endonuclease]]
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[[Category: integrase]]
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[[Category: Integrase]]
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[[Category: polynucleotidyl transferase]]
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[[Category: Polynucleotidyl transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:20:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:58:10 2008''
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Revision as of 08:20, 2 May 2008

Template:STRUCTURE 1bcm

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 Page seeded by OCA on Fri May 2 11:20:37 2008

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