1bco - Revision history

OCA at 06:35, 7 February 2024

2024-02-07T06:35:13Z

← Older revision		Revision as of 06:35, 7 February 2024
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	<StructureSection load='1bco' size='340' side='right'caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1bco' size='340' side='right'caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bpmu Bpmu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1BCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~MUA (AMINO ACIDS 248~~-~~574) (~~[~~http://www.ncbi~~.~~nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5~~&~~id=10677 BPMU])~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [~~http~~://pdbe.org/1bco PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1bco PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1bco ProSAT]</span></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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [https://pdbe.org/1bco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [https://www.ebi.ac.uk/pdbsum/1bco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~TRA_BPMU TRA_BPMU~~]~~] This transposase is essential~~ for integration, replication-transposition, and ~~excision~~ of Mu DNA.		[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 ==		== 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=1bco 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=1bco ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4 A resolution. The first of two subdomains contains the active site and, despite very limited sequence homology, exhibits a striking similarity to the core domain of HIV-1 integrase, which carries out a similar set of biochemical reactions. It also exhibits more limited similarity to other nucleases, RNase H and RuvC. The second, a beta barrel, connects to the first subdomain through several contacts. Three independent determinations of the monomer structure from two crystal forms all show the active site held in a similar, apparently inactive configuration. The enzymatic activity of MuA is known to be activated by formation of a DNA-bound tetramer of the protein. We propose that the connections between the two subdomains may be involved in the cross-talk between the active site and the other domains of the transposase that controls the activity of the protein.

	Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration.,Rice P, Mizuuchi K Cell. 1995 Jul 28;82(2):209-20. PMID:7628012<ref>PMID:7628012</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Transposase 3D structures\|Transposase 3D structures]]		*[[Transposase 3D structures\|Transposase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bpmu~~]]		[[Category: Escherichia virus Mu]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Mizuuchi, K]]		[[Category: Mizuuchi K]]
	[[Category: Rice~~, P A]]~~		[[Category: Rice PA]]
	~~[[Category: Dna binding]]~~
	~~[[Category: Endonuclease]]~~
	~~[[Category: Integrase]]~~
	~~[[Category: Polynucleotidyl transferase]]~~
	~~[[Category: Transposase~~]]

OCA at 10:13, 18 November 2020

2020-11-18T10:13:22Z

← Older revision		Revision as of 10:13, 18 November 2020
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	==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN==		==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN==
	<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1bco' size='340' side='right'caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://pdbe.org/1bco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bco ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://pdbe.org/1bco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bco_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/1bco_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Transposase 3D structures\|Transposase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Bpmu]]		[[Category: Bpmu]]
			[[Category: Large Structures]]
	[[Category: Mizuuchi, K]]		[[Category: Mizuuchi, K]]
	[[Category: Rice, P A]]		[[Category: Rice, P A]]

OCA at 11:18, 22 November 2017

2017-11-22T11:18:37Z

← Older revision		Revision as of 11:18, 22 November 2017
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	==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN==		==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN==
	<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>
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	<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://pdbe.org/1bco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco 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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://pdbe.org/1bco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bco ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Transposase\|Transposase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 01:27, 10 February 2016

2016-02-10T01:27:24Z

← Older revision		Revision as of 01:27, 10 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ 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=1bco ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:00, 11 September 2015

2015-09-11T04:00:26Z

← Older revision		Revision as of 04:00, 11 September 2015
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	<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with 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=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 ~~Enterobacteria phage Mu~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco 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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://pdbe.org/1bco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 1bco" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Enterobacteria phage mu~~]]		[[Category: Bpmu]]
	[[Category: Mizuuchi, K]]		[[Category: Mizuuchi, K]]
	[[Category: Rice, P A]]		[[Category: Rice, P A]]

OCA at 10:51, 25 December 2014

2014-12-25T10:51:01Z

← Older revision		Revision as of 10:51, 25 December 2014
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	<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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco 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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/TRA_BPMU TRA_BPMU]] This transposase is essential for integration, replication-transposition, and excision of Mu DNA.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:43, 22 December 2014

2014-12-22T11:43:01Z

← Older revision		Revision as of 11:43, 22 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with 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=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>		<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with 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=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu])</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco 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=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Enterobacteria phage mu]]		[[Category: Enterobacteria phage mu]]
	[[Category: Mizuuchi, K.]]		[[Category: Mizuuchi, K]]
	[[Category: Rice, P A.]]		[[Category: Rice, P A]]
	[[Category: Dna binding]]		[[Category: Dna binding]]
	[[Category: Endonuclease]]		[[Category: Endonuclease]]

OCA at 11:39, 3 October 2014

2014-10-03T11:39:19Z

← Older revision		Revision as of 11:39, 3 October 2014
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>

			==See Also==
			*[[Transposase\|Transposase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:22, 7 August 2014

2014-08-07T03:22:42Z

← Older revision		Revision as of 03:22, 7 August 2014
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	[[Image:~~1bco~~.~~png~~\|~~left~~\|~~200px~~]]		==BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN==
			<StructureSection load='1bco' size='340' side='right' caption='[[1bco]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1bco]] is a 1 chain structure with 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=1BCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BCO FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUA (AMINO ACIDS 248-574) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu])</td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bco RCSB], [http://www.ebi.ac.uk/pdbsum/1bco PDBsum]</span></td></tr>
			<table>
			== 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/bc/1bco_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/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4 A resolution. The first of two subdomains contains the active site and, despite very limited sequence homology, exhibits a striking similarity to the core domain of HIV-1 integrase, which carries out a similar set of biochemical reactions. It also exhibits more limited similarity to other nucleases, RNase H and RuvC. The second, a beta barrel, connects to the first subdomain through several contacts. Three independent determinations of the monomer structure from two crystal forms all show the active site held in a similar, apparently inactive configuration. The enzymatic activity of MuA is known to be activated by formation of a DNA-bound tetramer of the protein. We propose that the connections between the two subdomains may be involved in the cross-talk between the active site and the other domains of the transposase that controls the activity of the protein.

	~~{{STRUCTURE_1bco\| PDB=1bco \| SCENE= }}~~		Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration.,Rice P, Mizuuchi K Cell. 1995 Jul 28;82(2):209-20. PMID:7628012<ref>PMID:7628012</ref>

	~~===BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_7628012}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[1bco]] is~~ a ~~1 chain structure with 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=1BCO OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:007628012<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Enterobacteria phage mu]]		[[Category: Enterobacteria phage mu]]
	[[Category: Mizuuchi, K.]]		[[Category: Mizuuchi, K.]]

OCA: Protected "1bco" [edit=sysop:move=sysop]

2012-10-21T14:29:12Z

Protected "1bco" [edit=sysop:move=sysop]

← Older revision	Revision as of 14:29, 21 October 2012
(No difference)