1x1p

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[[Image:1x1p.gif|left|200px]]<br /><applet load="1x1p" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1x1p, resolution 2.80&Aring;" />
 
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'''Crystal structure of Tk-RNase HII(1-197)-A(28-42)'''<br />
 
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==Overview==
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==Crystal structure of Tk-RNase HII(1-197)-A(28-42)==
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Conformational studies on amyloid beta peptide (Abeta) in aqueous solution are complicated by its tendency to aggregate. In this study, we determined the atomic-level structure of Abeta(28-42) in an aqueous environment. We fused fragments of Abeta, residues 10-24 (Abeta(10-24)) or 28-42 (Abeta(28-42)), to three positions in the C-terminal region of ribonuclease HII from a hyperthermophile, Thermococcus kodakaraensis (Tk-RNase HII). We then examined the structural properties in an aqueous environment. The host protein, Tk-RNase HII, is highly stable and the C-terminal region has relatively little interaction with other parts. CD spectroscopy and thermal denaturation experiments demonstrated that the guest amyloidogenic sequences did not affect the overall structure of the Tk-RNase HII. Crystal structure analysis of Tk-RNase HII(1-197)-Abeta(28-42) revealed that Abeta(28-42) forms a beta conformation, whereas the original structure in Tk-RNase HII(1-213) was alpha helix, suggesting beta-structure formation of Abeta(28-42) within full-length Abeta in aqueous solution. Abeta(28-42) enhanced aggregation of the host protein more strongly than Abeta(10-24). These results and other reports suggest that after proteolytic cleavage, the C-terminal region of Abeta adopts a beta conformation in an aqueous environment and induces aggregation, and that the central region of Abeta plays a critical role in fibril formation. This study also indicates that this fusion technique is useful for obtaining structural information with atomic resolution for amyloidogenic peptides in aqueous environments.
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<StructureSection load='1x1p' size='340' side='right'caption='[[1x1p]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1x1p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X1P 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]] 2.8&#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=1x1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1p OCA], [https://pdbe.org/1x1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x1p RCSB], [https://www.ebi.ac.uk/pdbsum/1x1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x1p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNH2_THEKO RNH2_THEKO] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x1p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1x1p ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1X1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1X1P OCA].
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of amyloid beta fragments in aqueous environments., Takano K, Endo S, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S, FEBS J. 2006 Jan;273(1):150-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16367755 16367755]
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[[Category: Large Structures]]
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[[Category: Ribonuclease H]]
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[[Category: Thermococcus kodakarensis KOD1]]
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[[Category: Single protein]]
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[[Category: Chon H]]
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[[Category: Thermococcus kodakarensis]]
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[[Category: Endo S]]
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[[Category: Chon, H.]]
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[[Category: Kanaya S]]
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[[Category: Endo, S.]]
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[[Category: Koga Y]]
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[[Category: Kanaya, S.]]
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[[Category: Matsumura H]]
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[[Category: Koga, Y.]]
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[[Category: Mukaiyama A]]
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[[Category: Matsumura, H.]]
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[[Category: Takano K]]
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[[Category: Mukaiyama, A.]]
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[[Category: Takano, K.]]
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[[Category: amyloid peptide]]
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[[Category: ribonuclease hii]]
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[[Category: thermococcus kodakaraensis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:10 2008''
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Current revision

Crystal structure of Tk-RNase HII(1-197)-A(28-42)

PDB ID 1x1p

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