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| - | [[Image:1f6v.jpg|left|200px]]<br /><applet load="1f6v" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1f6v" /> | |
| - | '''SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN'''<br /> | |
| | | | |
| - | ==Overview== | + | ==SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN== |
| - | Mu B is one of four proteins required for the strand transfer step of bacteriophage Mu DNA transposition and the only one where no high resolution structural data is available. Structural work on Mu B has been hampered primarily by solubility problems and its tendency to aggregate. We have overcome this problem by determination of the three-dimensional structure of the C-terminal domain of Mu B (B(223-312)) in 1.5 M NaCl using NMR spectroscopic methods. The structure of Mu B(223-312) comprises four helices (backbone r.m.s.d. 0.46 A) arranged in a loosely packed bundle and resembles that of the N-terminal region of the replication helicase, DnaB. This structural motif is likely to be involved in the inter-domainal regulation of ATPase activity for both Mu A and DnaB. The approach described here for structural determination in high salt may be generally applicable for proteins that do not crystallize and that are plagued by solubility problems at low ionic strength.
| + | <StructureSection load='1f6v' size='340' side='right'caption='[[1f6v]]' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1f6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F6V FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6v OCA], [https://pdbe.org/1f6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f6v RCSB], [https://www.ebi.ac.uk/pdbsum/1f6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6v ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TARGB_BPMU TARGB_BPMU] Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-primed replication over integration. Prevents self-integration into an integrated copy of the viral genome. This mechanism is called target immunity and is achieved by two mechanisms: first, the target DNA activator B dissociates from the viral genome ends upon interaction in cis with DDE-recombinase A, which makes the viral genome ends a poor target for new insertions. Second, the interior of the viral genome may also ne protected from integration events by the target DNA activator B being strongly bound throughout the whole viral genome.<ref>PMID:11298282</ref> <ref>PMID:14661976</ref> <ref>PMID:1646076</ref> <ref>PMID:17709741</ref> <ref>PMID:17988683</ref> <ref>PMID:20226074</ref> <ref>PMID:23776210</ref> <ref>PMID:24478936</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/f6/1f6v_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=1f6v ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | ==About this Structure== | + | ==See Also== |
| - | 1F6V 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=1F6V OCA].
| + | *[[Transposase 3D structures|Transposase 3D structures]] |
| - | | + | == References == |
| - | ==Reference== | + | <references/> |
| - | The solution structure of the C-terminal domain of the Mu B transposition protein., Hung LH, Chaconas G, Shaw GS, EMBO J. 2000 Nov 1;19(21):5625-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11060014 11060014]
| + | __TOC__ |
| - | [[Category: Enterobacteria phage mu]] | + | </StructureSection> |
| - | [[Category: Single protein]] | + | [[Category: Escherichia virus Mu]] |
| - | [[Category: Chaconas, G.]] | + | [[Category: Large Structures]] |
| - | [[Category: Hung, L-H]] | + | [[Category: Chaconas G]] |
| - | [[Category: Shaw, G S.]] | + | [[Category: Hung L-H]] |
| - | [[Category: atpase]]
| + | [[Category: Shaw GS]] |
| - | [[Category: dna binding]]
| + | |
| - | [[Category: high salt]]
| + | |
| - | [[Category: mu phage]]
| + | |
| - | [[Category: nmr]]
| + | |
| - | [[Category: recombination]]
| + | |
| - | [[Category: solution structure]]
| + | |
| - | [[Category: transposition]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:31 2008''
| + | |
| Structural highlights
Function
TARGB_BPMU Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-primed replication over integration. Prevents self-integration into an integrated copy of the viral genome. This mechanism is called target immunity and is achieved by two mechanisms: first, the target DNA activator B dissociates from the viral genome ends upon interaction in cis with DDE-recombinase A, which makes the viral genome ends a poor target for new insertions. Second, the interior of the viral genome may also ne protected from integration events by the target DNA activator B being strongly bound throughout the whole viral genome.[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.
See Also
References
- ↑ Roldan LA, Baker TA. Differential role of the Mu B protein in phage Mu integration vs. replication: mechanistic insights into two transposition pathways. Mol Microbiol. 2001 Apr;40(1):141-55. PMID:11298282
- ↑ Goldhaber-Gordon I, Early MH, Baker TA. MuA transposase separates DNA sequence recognition from catalysis. Biochemistry. 2003 Dec 16;42(49):14633-42. PMID:14661976 doi:http://dx.doi.org/10.1021/bi035360o
- ↑ Baker TA, Mizuuchi M, Mizuuchi K. MuB protein allosterically activates strand transfer by the transposase of phage Mu. Cell. 1991 Jun 14;65(6):1003-13. PMID:1646076
- ↑ Tan X, Mizuuchi M, Mizuuchi K. DNA transposition target immunity and the determinants of the MuB distribution patterns on DNA. Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13925-9. Epub 2007 Aug 20. PMID:17709741 doi:http://dx.doi.org/10.1073/pnas.0706564104
- ↑ Lemberg KM, Schweidenback CT, Baker TA. The dynamic Mu transpososome: MuB activation prevents disintegration. J Mol Biol. 2007 Dec 14;374(5):1158-71. Epub 2007 Oct 3. PMID:17988683 doi:http://dx.doi.org/10.1016/j.jmb.2007.09.079
- ↑ Ge J, Lou Z, Harshey RM. Immunity of replicating Mu to self-integration: a novel mechanism employing MuB protein. Mob DNA. 2010 Feb 1;1(1):8. doi: 10.1186/1759-8753-1-8. PMID:20226074 doi:http://dx.doi.org/10.1186/1759-8753-1-8
- ↑ Mizuno N, Dramicanin M, Mizuuchi M, Adam J, Wang Y, Han YW, Yang W, Steven AC, Mizuuchi K, Ramon-Maiques S. MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition. Proc Natl Acad Sci U S A. 2013 Jun 17. PMID:23776210 doi:10.1073/pnas.1309499110
- ↑ Dramicanin M, Ramon-Maiques S. MuB gives a new twist to target DNA selection. Mob Genet Elements. 2013 Sep 1;3(5):e27515. Epub 2013 Dec 12. PMID:24478936 doi:http://dx.doi.org/10.4161/mge.27515
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