2ezh

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE

Structural highlights

2ezh 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

TNPA_BPMU Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair. Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE-recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target-primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome. Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication.

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

The MuA transposase of phase Mu is a large modular protein that plays a central role in transposition. We show that the Mu end DNA-binding domain, I beta gamma, which is responsible for binding the DNA attachment sites at each end of the Mu genome, comprises two subdomains, I beta and I gamma, that are structurally autonomous and do not interact with each other in the absence of DNA. The solution structure of the I gamma subdomain has been determined by multidimensional NMR spectroscopy. The structure of I gamma comprises a four helix bundle and, despite the absence of any significant sequence identity, the topology of the first three helices is very similar to that of the homeodomain family of helix-turn-helix DNA-binding proteins. The helix-turn-helix motif of I gamma, however, differs from that of the homeodomains in so far as the loop is longer and the second helix is shorter, reminiscent of that in the POU-specific domain.

Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase.,Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM J Mol Biol. 1997 Oct 17;273(1):19-25. PMID:9367742^[1]

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

References

↑ Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM. Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase. J Mol Biol. 1997 Oct 17;273(1):19-25. PMID:9367742 doi:10.1006/jmbi.1997.1312

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ezh"

@@ Line 1: / Line 1: @@
-[[Image:2ezh.gif|left|200px]]<br /><applet load="2ezh" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2ezh" />
-'''SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE'''<br />
-==Overview==
+==SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE==
-The MuA transposase of phase Mu is a large modular protein that plays a, central role in transposition. We show that the Mu end DNA-binding domain, I beta gamma, which is responsible for binding the DNA attachment sites at, each end of the Mu genome, comprises two subdomains, I beta and I gamma, that are structurally autonomous and do not interact with each other in, the absence of DNA. The solution structure of the I gamma subdomain has, been determined by multidimensional NMR spectroscopy. The structure of I, gamma comprises a four helix bundle and, despite the absence of any, significant sequence identity, the topology of the first three helices is, very similar to that of the homeodomain family of helix-turn-helix, DNA-binding proteins. The helix-turn-helix motif of I gamma, however, differs from that of the homeodomains in so far as the loop is longer and, the second helix is shorter, reminiscent of that in the POU-specific, domain.
+<StructureSection load='2ezh' size='340' side='right'caption='[[2ezh]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ezh]] 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=2EZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZH 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=2ezh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezh OCA], [https://pdbe.org/2ezh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ezh RCSB], [https://www.ebi.ac.uk/pdbsum/2ezh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ezh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TNPA_BPMU TNPA_BPMU] Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by the DDE-recombinase A endonuclease activity, with the help of host chaperone ClpX. The gaps created in the host chromosome by the viral genome insertion are repaired by the host primary machinery for double-strand break repair.  Responsible for replication of the viral genome by replicative transposition. During replicative transposition, DDE-recombinase A is part of the transpososome complex. DDE-recombinase A cleaves the viral DNA and the resulting 3'-OH performs a nucleophilic attack of the host DNA. The 5' flanking DNA is not resected and an intermediary structure is formed. This structure is resolved by target-primed replication leading to two copies of the viral genome (the original one and the copied one). Host ClpX and translation initiation factor IF2 play an essential transpososome-remodeling role by releasing the block between transposition and DNA replication. Successive rounds of replicative transposition can lead up to 100 copies of the viral genome.  Promotes replication and thereby lytic development by competing with repressor c (Repc) for binding to the internal activation sequence (IAS) in the enhancer/operator region. The outcome of this competition determines if the virus enters latency or starts replication.
+== 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/ez/2ezh_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=2ezh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The MuA transposase of phase Mu is a large modular protein that plays a central role in transposition. We show that the Mu end DNA-binding domain, I beta gamma, which is responsible for binding the DNA attachment sites at each end of the Mu genome, comprises two subdomains, I beta and I gamma, that are structurally autonomous and do not interact with each other in the absence of DNA. The solution structure of the I gamma subdomain has been determined by multidimensional NMR spectroscopy. The structure of I gamma comprises a four helix bundle and, despite the absence of any significant sequence identity, the topology of the first three helices is very similar to that of the homeodomain family of helix-turn-helix DNA-binding proteins. The helix-turn-helix motif of I gamma, however, differs from that of the homeodomains in so far as the loop is longer and the second helix is shorter, reminiscent of that in the POU-specific domain.
-==About this Structure==
+Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase.,Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM J Mol Biol. 1997 Oct 17;273(1):19-25. PMID:9367742<ref>PMID:9367742</ref>
-EZH 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EZH OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase., Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Clore GM, J Mol Biol. 1997 Oct 17;273(1):19-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9367742 9367742]
+</div>
-[[Category: Enterobacteria phage mu]]
+<div class="pdbe-citations 2ezh" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Clore, G.M.]]
-[[Category: Clubb, R.T.]]
-[[Category: Gronenborn, A.M.]]
-[[Category: Schumaker, S.]]
-[[Category: dna-binding protein]]
-[[Category: transposition]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:15:06 2007''
+==See Also==
+*[[Transposase 3D structures|Transposase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia virus Mu]]
+[[Category: Large Structures]]
+[[Category: Clore GM]]
+[[Category: Clubb RT]]
+[[Category: Gronenborn AM]]
+[[Category: Schumaker S]]

2ezh

From Proteopedia

Current revision

SOLUTION NMR STRUCTURE OF THE IGAMMA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF MU PHAGE TRANSPOSASE, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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