View source for 1bcm


==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT==
<StructureSection load='1bcm' size='340' side='right'caption='[[1bcm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bcm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BCM FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248 - 574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcm OCA], [http://pdbe.org/1bcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bcm RCSB], [http://www.ebi.ac.uk/pdbsum/1bcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bcm ProSAT]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/TRA_BPMU TRA_BPMU]] This transposase is essential for integration, replication-transposition, and excision of Mu DNA. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bcm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bcm ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:7628012</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Transposase 3D structures|Transposase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bpmu]]
[[Category: Large Structures]]
[[Category: Mizuuchi, K]]
[[Category: Rice, P A]]
[[Category: Dna binding]]
[[Category: Endonuclease]]
[[Category: Integrase]]
[[Category: Polynucleotidyl transferase]]
[[Category: Transposase]]