1f6v: Difference between revisions

Latest revision as of 10:11, 20 March 2024

SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN

Structural highlights

1f6v is a 1 chain structure with sequence from Escherichia virus Mu. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.4161/mge.27515

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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:https://dx.doi.org/10.1021/bi035360o

[3] 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

[4] 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:https://dx.doi.org/10.1073/pnas.0706564104

[5] 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:https://dx.doi.org/10.1016/j.jmb.2007.09.079

[6] 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:https://dx.doi.org/10.1186/1759-8753-1-8

[7] 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

[8] 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:https://dx.doi.org/10.4161/mge.27515

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@@ Line 1: / Line 1: @@
-[[Image:1f6v.png|left|200px]]
-{{STRUCTURE_1f6v|  PDB=1f6v  |  SCENE=  }}
+==SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN==
+<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>
-===SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN===
+==See Also==
+*[[Transposase 3D structures|Transposase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-[[1f6v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6V OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Escherichia virus Mu]]
-<ref group="xtra">PMID:011060014</ref><references group="xtra"/>
+[[Category: Large Structures]]
-[[Category: Enterobacteria phage mu]]
+[[Category: Chaconas G]]
-[[Category: Chaconas, G.]]
+[[Category: Hung L-H]]
-[[Category: Hung, L-H]]
+[[Category: Shaw GS]]
-[[Category: Shaw, G S.]]
-[[Category: Atpase]]
-[[Category: Dna binding]]
-[[Category: Dna binding protein]]
-[[Category: High salt]]
-[[Category: Mu phage]]
-[[Category: Recombination]]
-[[Category: Solution structure]]
-[[Category: Transposition]]

1f6v: Difference between revisions

Latest revision as of 10:11, 20 March 2024

SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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