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1hh2: Difference between revisions

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[[Image:1hh2.jpg|left|200px]]


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==Crystal structure of NusA from Thermotoga maritima==
The line below this paragraph, containing "STRUCTURE_1hh2", creates the "Structure Box" on the page.
<StructureSection load='1hh2' size='340' side='right'caption='[[1hh2]], [[Resolution|resolution]] 2.10&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'>[[1hh2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HH2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hh2 OCA], [https://pdbe.org/1hh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hh2 RCSB], [https://www.ebi.ac.uk/pdbsum/1hh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hh2 ProSAT]</span></td></tr>
{{STRUCTURE_1hh2| PDB=1hh2  | SCENE= }}
</table>
 
== Function ==
'''CRYSTAL STRUCTURE OF NUSA FROM THERMOTOGA MARITIMA'''
[https://www.uniprot.org/uniprot/Q9X298_THEMA Q9X298_THEMA]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/1hh2_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=1hh2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding.
The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding.


==About this Structure==
An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.,Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC Mol Cell. 2001 Jun;7(6):1177-89. PMID:11430821<ref>PMID:11430821</ref>
1HH2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA., Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC, Mol Cell. 2001 Jun;7(6):1177-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11430821 11430821]
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[[Category: Single protein]]
<div class="pdbe-citations 1hh2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Bartunik, H D.]]
[[Category: Bartunik HD]]
[[Category: Bourenkov, G P.]]
[[Category: Bourenkov GP]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Wahl, M C.]]
[[Category: Wahl MC]]
[[Category: Worbs, M.]]
[[Category: Worbs M]]
[[Category: Termination]]
[[Category: Transcription regulation]]
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