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[[Image:1h7m.gif|left|200px]]<br /><applet load="1h7m" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1h7m, resolution 1.96&Aring;" />
'''RIBOSOMAL PROTEIN L30E FROM THERMOCOCCUS CELER'''<br />


==Overview==
==Ribosomal Protein L30e from Thermococcus celer==
We report here the high-resolution crystal structure of the ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer determined at cryo-temperature. When it is compared with its mesophilic homologue, L30e from yeast, a number of structural features that can enhance thermostability are revealed. Disordered residues corresponding to a large RNA-binding loop in yeast L30e are well structured in the T. celer protein. The overall charge of T. celer L30e is near neutral, whereas that of the yeast homologue is highly positive. This is the result of an increase in the number of acidic residues at the expense of polar residues, Asn, Ser, and Thr. Extensive ion pair networks are found on the molecular surface. Exposed nonpolar surface areas are reduced in the T. celer protein. Its side chain atoms preferably form hydrogen bonds with main chain atoms. Taken together, these factors contribute to high protein stability. The roles of well-conserved L30e residues are studied and found to be important in defining a very compact overall structure and in maintaining the structure of the RNA binding site. By comparing it with the yeast homologue, we also identified the residues that are responsible for RNA binding and built a model to illustrate how L30e binds to an RNA kink turn motif.
<StructureSection load='1h7m' size='340' side='right'caption='[[1h7m]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H7M 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]] 1.96&#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=1h7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h7m OCA], [https://pdbe.org/1h7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h7m RCSB], [https://www.ebi.ac.uk/pdbsum/1h7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h7m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
== 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/h7/1h7m_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=1h7m ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1H7M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H7M OCA].
*[[Kink-turn motif|Kink-turn motif]]
 
*[[Ribosomal protein L30|Ribosomal protein L30]]
==Reference==
*[[User:Wayne Decatur/kink-turn motif|User:Wayne Decatur/kink-turn motif]]
Crystal structure of ribosomal protein L30e from the extreme thermophile Thermococcus celer: thermal stability and RNA binding., Chen YW, Bycroft M, Wong KB, Biochemistry. 2003 Mar 18;42(10):2857-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12627951 12627951]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus celer]]
[[Category: Thermococcus celer]]
[[Category: Chen, Y W.]]
[[Category: Chen YW]]
[[Category: Wong, K B.]]
[[Category: Wong KB]]
[[Category: ribosomal protein]]
[[Category: ribosome]]
[[Category: rna-binding]]
[[Category: thermophilic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:17 2008''

Latest revision as of 14:29, 27 March 2024

Ribosomal Protein L30e from Thermococcus celerRibosomal Protein L30e from Thermococcus celer

Structural highlights

1h7m is a 1 chain structure with sequence from Thermococcus celer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.96Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL30E_THECE

Evolutionary Conservation

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

See Also

1h7m, resolution 1.96Å

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