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[[Image:1x1p.gif|left|200px]]<br /><applet load="1x1p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1x1p, resolution 2.80&Aring;" />
'''Crystal structure of Tk-RNase HII(1-197)-A(28-42)'''<br />


==Overview==
==Crystal structure of Tk-RNase HII(1-197)-A(28-42)==
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.
<StructureSection load='1x1p' size='340' side='right'caption='[[1x1p]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNH2_THEKO RNH2_THEKO] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
== 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/x1/1x1p_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=1x1p ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Large Structures]]
[[Category: Ribonuclease H]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Single protein]]
[[Category: Chon H]]
[[Category: Thermococcus kodakarensis]]
[[Category: Endo S]]
[[Category: Chon, H.]]
[[Category: Kanaya S]]
[[Category: Endo, S.]]
[[Category: Koga Y]]
[[Category: Kanaya, S.]]
[[Category: Matsumura H]]
[[Category: Koga, Y.]]
[[Category: Mukaiyama A]]
[[Category: Matsumura, H.]]
[[Category: Takano K]]
[[Category: Mukaiyama, A.]]
[[Category: Takano, K.]]
[[Category: amyloid peptide]]
[[Category: ribonuclease hii]]
[[Category: thermococcus kodakaraensis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:50:10 2008''

Latest revision as of 16:35, 13 March 2024

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

Structural highlights

1x1p is a 1 chain structure with sequence from Thermococcus kodakarensis KOD1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNH2_THEKO Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1x1p, resolution 2.80Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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