View source for 1muh


==CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA==
<StructureSection load='1muh' size='340' side='right' caption='[[1muh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1muh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1f3i 1f3i]. The December 2006 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Transposase''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2006_12 10.2210/rcsb_pdb/mom_2006_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MUH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1muh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1muh OCA], [http://pdbe.org/1muh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1muh RCSB], [http://www.ebi.ac.uk/pdbsum/1muh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1muh ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX]] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref>  
== 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/mu/1muh_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=1muh ConSurf].
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== Publication Abstract from PubMed ==
Genomic evolution has been profoundly influenced by DNA transposition, a process whereby defined DNA segments move freely about the genome. Transposition is mediated by transposases, and similar events are catalyzed by retroviral integrases such as human immunodeficiency virus-1 (HIV-1) integrase. Understanding how these proteins interact with DNA is central to understanding the molecular basis of transposition. We report the three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA determined to 2.3 angstrom resolution. The molecular assembly is dimeric, where each double-stranded DNA molecule is bound by both protein subunits, orienting the transposon ends into the active sites. This structure provides a molecular framework for understanding many aspects of transposition, including the binding of transposon end DNA by one subunit and cleavage by a second, cleavage of two strands of DNA by a single active site via a hairpin intermediate, and strand transfer into target DNA.

Three-dimensional structure of the Tn5 synaptic complex transposition intermediate.,Davies DR, Goryshin IY, Reznikoff WS, Rayment I Science. 2000 Jul 7;289(5476):77-85. PMID:10884228<ref>PMID:10884228</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1muh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Transposase]]
[[Category: Davies, D R]]
[[Category: Goryshin, I Y]]
[[Category: Holden, H M]]
[[Category: Rayment, I]]
[[Category: Reznikoff, W S]]
[[Category: Thoden, J B]]
[[Category: Protein-dna complex]]
[[Category: Ribonuclease h-like motif]]
[[Category: Synaptic complex]]
[[Category: Transcription-dna complex]]