1muh

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(Difference between revisions)

Revision as of 07:41, 31 January 2018

CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA

Structural highlights

1muh is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1f3i. The December 2006 RCSB PDB Molecule of the Month feature on Transposase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rothstein SJ, Reznikoff WS. The functional differences in the inverted repeats of Tn5 are caused by a single base pair nonhomology. Cell. 1981 Jan;23(1):191-9. PMID:6260374
↑ Johnson RC, Yin JC, Reznikoff WS. Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat. Cell. 1982 Oct;30(3):873-82. PMID:6291786
↑ Lowe JB, Berg DE. A product of the TN5 transposase gene inhibits transposition. Genetics. 1983 Apr;103(4):605-15. PMID:6303899
↑ Wiegand TW, Reznikoff WS. Characterization of two hypertransposing Tn5 mutants. J Bacteriol. 1992 Feb;174(4):1229-39. PMID:1310499
↑ de la Cruz NB, Weinreich MD, Wiegand TW, Krebs MP, Reznikoff WS. Characterization of the Tn5 transposase and inhibitor proteins: a model for the inhibition of transposition. J Bacteriol. 1993 Nov;175(21):6932-8. PMID:8226636
↑ York D, Reznikoff WS. Purification and biochemical analyses of a monomeric form of Tn5 transposase. Nucleic Acids Res. 1996 Oct 1;24(19):3790-6. PMID:8871560
↑ Naumann TA, Reznikoff WS. Tn5 transposase active site mutants. J Biol Chem. 2002 May 17;277(20):17623-9. Epub 2002 Mar 4. PMID:11877443 doi:10.1074/jbc.M200742200
↑ Steiniger-White M, Bhasin A, Lovell S, Rayment I, Reznikoff WS. Evidence for "unseen" transposase--DNA contacts. J Mol Biol. 2002 Oct 4;322(5):971-82. PMID:12367522
↑ Davies DR, Goryshin IY, Reznikoff WS, Rayment I. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate. Science. 2000 Jul 7;289(5476):77-85. PMID:10884228

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1muh"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 4: / Line 5: @@
 <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]</span></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 ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1muh_consurf.spt"</scriptWhenChecked>
+    <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>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1muh" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Transposase|Transposase]]
 == References ==
 <references/>

1muh

From Proteopedia

Revision as of 07:41, 31 January 2018

CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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