1a62: Difference between revisions

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~~[[Image:1a62.gif|left|200px]]<br /><applet load="1a62" size="450" color="white" frame="true" align="right" spinBox="true"~~

~~caption="1a62, resolution 1.55Å" />~~

~~'''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO'''<br />~~

==~~Overview~~==

==CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO==

Transcription termination factor rho is an ATP-dependent hexameric, helicase found in most eubacterial species. The Escherichia coli rho, monomer consists of two domains, an RNA-binding domain (residues 1-130), and an ATPase domain (residues 131-419). The ATPase domain is homologous, to the beta subunit of F1-ATPase. Here, we report that the crystal, structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms, that rho130 contains the oligosaccharide/oligonucleotide-binding (OB), fold, a five stranded beta-barrel. The beta-barrel of rho130 is also, surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending, the applicability of F1 ATPase as a structural model for hexameric rho.

== Structural highlights ==

<table><tr><td colspan='2'>[[1a62]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A62 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a62 OCA], [https://pdbe.org/1a62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a62 RCSB], [https://www.ebi.ac.uk/pdbsum/1a62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a62 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/RHO_ECOLI RHO_ECOLI] Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884]

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a62_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1a62 ConSurf].

== Publication Abstract from PubMed ==

Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho.

~~==About this Structure==~~

Crystal structure of the RNA-binding domain from transcription termination factor rho.,Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995<ref>PMID:9586995</ref>

~~1A62 is a [http://en.wikipedia.org/wiki/Single_protein Single protein]~~ structure of ~~sequence~~ from ~~[http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http~~:/~~/ispc.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA].~~

~~==Reference==~~

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

~~Crystal structure of the RNA-binding domain from transcription termination factor rho., Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS, Nat Struct Biol. 1998 May~~;~~5(5):352-6. PMID:[http:~~/~~/ispc.weizmann.ac.il//pmbin/getpm?pmid=9586995 9586995]~~

</div>

~~[[Category: Escherichia coli]]~~

~~[[Category: Single protein]]~~

~~[[Category: Allison~~, T.J.]]

~~[[Category: Briercheck, D.M~~.]]

~~[[Category: Rastinejad, F.]]~~

~~[[Category: Richardson, J.P.]]~~

~~[[Category: Rule, G.S.]]~~

~~[[Category: Wood, T.C.]]~~

~~[[Category: f1~~-~~atpase]]~~

~~[[Category~~: ~~ob fold]]~~

~~[[Category: rna binding domain]]~~

~~[[Category: termination]]~~

~~[[Category: transcription regulation]]~~

~~[[Category: transcription termination]]~~

~~''Page seeded by~~ [~~http:~~//~~ispc.weizmann.ac.il/oca OCA~~ ] ~~on Tue Nov 20 10~~:37:~~59 2007''~~

==See Also==

*[[Helicase 3D structures|Helicase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Allison TJ]]

[[Category: Briercheck DM]]

[[Category: Rastinejad F]]

[[Category: Richardson JP]]

[[Category: Rule GS]]

[[Category: Wood TC]]

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@@ Line 1: / Line 1: @@
-[[Image:1a62.gif|left|200px]]<br /><applet load="1a62" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1a62, resolution 1.55&Aring;" />
-'''CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE TRANSCRIPTIONAL TERMINATOR PROTEIN RHO==
-Transcription termination factor rho is an ATP-dependent hexameric, helicase found in most eubacterial species. The Escherichia coli rho, monomer consists of two domains, an RNA-binding domain (residues 1-130), and an ATPase domain (residues 131-419). The ATPase domain is homologous, to the beta subunit of F1-ATPase. Here, we report that the crystal, structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms, that rho130 contains the oligosaccharide/oligonucleotide-binding (OB), fold, a five stranded beta-barrel. The beta-barrel of rho130 is also, surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending, the applicability of F1 ATPase as a structural model for hexameric rho.
+<StructureSection load='1a62' size='340' side='right'caption='[[1a62]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1a62]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A62 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a62 OCA], [https://pdbe.org/1a62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a62 RCSB], [https://www.ebi.ac.uk/pdbsum/1a62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a62 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RHO_ECOLI RHO_ECOLI] Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884]
+== 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/a6/1a62_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1a62 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho.
-==About this Structure==
+Crystal structure of the RNA-binding domain from transcription termination factor rho.,Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS Nat Struct Biol. 1998 May;5(5):352-6. PMID:9586995<ref>PMID:9586995</ref>
-A62 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A62 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of the RNA-binding domain from transcription termination factor rho., Allison TJ, Wood TC, Briercheck DM, Rastinejad F, Richardson JP, Rule GS, Nat Struct Biol. 1998 May;5(5):352-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9586995 9586995]
+</div>
-[[Category: Escherichia coli]]
+<div class="pdbe-citations 1a62" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Allison, T.J.]]
-[[Category: Briercheck, D.M.]]
-[[Category: Rastinejad, F.]]
-[[Category: Richardson, J.P.]]
-[[Category: Rule, G.S.]]
-[[Category: Wood, T.C.]]
-[[Category: f1-atpase]]
-[[Category: ob fold]]
-[[Category: rna binding domain]]
-[[Category: termination]]
-[[Category: transcription regulation]]
-[[Category: transcription termination]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:37:59 2007''
+==See Also==
+*[[Helicase 3D structures|Helicase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Allison TJ]]
+[[Category: Briercheck DM]]
+[[Category: Rastinejad F]]
+[[Category: Richardson JP]]
+[[Category: Rule GS]]
+[[Category: Wood TC]]