1f6v
From Proteopedia
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==SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN== | ==SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN== | ||
| - | <StructureSection load='1f6v' size='340' side='right' caption='[[1f6v | + | <StructureSection load='1f6v' size='340' side='right'caption='[[1f6v]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1f6v]] is a 1 chain structure with sequence from [ | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Transposase 3D structures|Transposase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia virus Mu]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chaconas G]] |
| - | + | [[Category: Hung L-H]] | |
| - | [[Category: | + | [[Category: Shaw GS]] |
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Current revision
SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN
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