2e4l: Difference between revisions

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New page: left|200px<br /><applet load="2e4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e4l, resolution 2.00Å" /> '''Thermodynamic and St...
 
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[[Image:2e4l.jpg|left|200px]]<br /><applet load="2e4l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2e4l, resolution 2.00&Aring;" />
'''Thermodynamic and Structural Analysis of Thermolabile RNase HI from Shewanella oneidensis MR-1'''<br />


==About this Structure==
==Thermodynamic and Structural Analysis of Thermolabile RNase HI from Shewanella oneidensis MR-1==
2E4L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E4L OCA].
<StructureSection load='2e4l' size='340' side='right'caption='[[2e4l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
[[Category: Ribonuclease H]]
== Structural highlights ==
[[Category: Shewanella oneidensis]]
<table><tr><td colspan='2'>[[2e4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4L FirstGlance]. <br>
[[Category: Single protein]]
</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&#8491;</td></tr>
[[Category: Chon, H.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4l OCA], [https://pdbe.org/2e4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4l RCSB], [https://www.ebi.ac.uk/pdbsum/2e4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4l ProSAT]</span></td></tr>
[[Category: Kanaya, S.]]
</table>
[[Category: Koga, Y.]]
== Function ==
[[Category: Matsumura, H.]]
[https://www.uniprot.org/uniprot/RNH_SHEON RNH_SHEON] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity).
[[Category: Tadokoro, T.]]
== Evolutionary Conservation ==
[[Category: Takano, K.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: You, D.J.]]
Check<jmol>
[[Category: endoribonuclease]]
  <jmolCheckbox>
[[Category: hydrolase]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/2e4l_consurf.spt"</scriptWhenChecked>
[[Category: rnase hi]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: shewanella oneidensis mr-1]]
    <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=2e4l ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease (RNase) HI from the psychrotrophic bacterium Shewanella oneidensis MR-1 was overproduced in Escherichia coli, purified, and structurally and biochemically characterized. The amino acid sequence of MR-1 RNase HI is 67% identical to that of E. coli RNase HI. The crystal structure of MR-1 RNase HI determined at 2.0 A resolution was highly similar to that of E. coli RNase HI, except that the number of intramolecular ion pairs and the fraction of polar surface area of MR-1 RNase HI were reduced compared to those of E. coli RNase HI. The enzymatic properties of MR-1 RNase HI were similar to those of E. coli RNase HI. However, MR-1 RNase HI was much less stable than E. coli RNase HI. The stability of MR-1 RNase HI against heat inactivation was lower than that of E. coli RNase HI by 19 degrees C. The conformational stability of MR-1 RNase HI was thermodynamically analyzed by monitoring the CD values at 220 nm. MR-1 RNase HI was less stable than E. coli RNase HI by 22.4 degrees C in Tm and 12.5 kJ/mol in DeltaG(H2O). The thermodynamic stability curve of MR-1 RNase HI was characterized by a downward shift and increased curvature, which results in an increased DeltaCp value, compared to that of E. coli RNase HI. Site-directed mutagenesis studies suggest that the difference in the number of intramolecular ion pairs partly accounts for the difference in stability between MR-1 and E. coli RNases HI.


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:56:29 2007''
Structural, thermodynamic, and mutational analyses of a psychrotrophic RNase HI.,Tadokoro T, You DJ, Abe Y, Chon H, Matsumura H, Koga Y, Takano K, Kanaya S Biochemistry. 2007 Jun 26;46(25):7460-8. Epub 2007 May 31. PMID:17536836<ref>PMID:17536836</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2e4l" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shewanella oneidensis MR-1]]
[[Category: Chon H]]
[[Category: Kanaya S]]
[[Category: Koga Y]]
[[Category: Matsumura H]]
[[Category: Tadokoro T]]
[[Category: Takano K]]
[[Category: You DJ]]
Retrieved from "https://proteopedia.org/2e4l"