3i32: Difference between revisions

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[[Image:3i32.jpg|left|200px]]


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==Dimeric structure of a Hera helicase fragment including the C-terminal RecA domain, the dimerization domain, and the RNA binding domain==
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<StructureSection load='3i32' size='340' side='right'caption='[[3i32]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3i32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I32 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
{{STRUCTURE_3i32|  PDB=3i32  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i32 OCA], [https://pdbe.org/3i32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i32 RCSB], [https://www.ebi.ac.uk/pdbsum/3i32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i32 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q72GF3_THET2 Q72GF3_THET2]
== 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/i3/3i32_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=3i32 ConSurf].
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== Publication Abstract from PubMed ==
DEAD box family helicases consist of a helicase core that is formed by two flexibly linked RecA-like domains. The helicase activity can be regulated by N- or C-terminal extensions flanking the core. Thermus thermophilus heat resistant RNA-dependent ATPase (Hera) is the first DEAD box helicase that forms a dimer using a unique dimerization domain. In addition to the dimerization domain, Hera contains a C-terminal RNA binding domain (RBD) that shares sequence homology only to uncharacterized proteins of the Deinococcus/Thermus group. The crystal structure of Hera_RBD reveals the fold of an altered RNA recognition motif (RRM) with limited structural homology to the RBD of the DEAD box helicase YxiN from Bacillus subtilis. Comparison with RRM/RNA complexes shows that a RNA binding mode different than that suggested for YxiN, but similar to U1A, can be inferred for Hera. The orientation of the RBD relative to the helicase core was defined in a second crystal structure of a Hera fragment including the C-terminal RecA domain, the dimerization domain, and the RBD. The structures allow construction of a model for the entire Hera helicase dimer. A likely binding surface for large RNA substrates that spans both RecA-like domains and the RBD is identified.


===Dimeric structure of a Hera helicase fragment including the C-terminal RecA domain, the dimerization domain, and the RNA binding domain===
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.,Rudolph MG, Klostermeier D RNA. 2009 Nov;15(11):1993-2001. Epub 2009 Aug 26. PMID:19710183<ref>PMID:19710183</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3i32" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19710183 is the PubMed ID number.
*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_19710183}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
3I32 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb27 Thermus thermophilus hb27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I32 OCA].
[[Category: Large Structures]]
 
[[Category: Thermus thermophilus HB27]]
==Reference==
[[Category: Klostermeier D]]
<ref group="xtra">PMID:19710183</ref><references group="xtra"/>
[[Category: Rudolph MG]]
[[Category: Thermus thermophilus hb27]]
[[Category: Klostermeier, D.]]
[[Category: Rudolph, M G.]]
[[Category: Atp-binding]]
[[Category: Atpase]]
[[Category: Dimer]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Nucleotide-binding]]
[[Category: Rna binding protein]]
[[Category: Rna helicase]]
[[Category: Rna recognition motif]]
 
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