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<StructureSection load='1bxy' size='340' side='right'caption='[[1bxy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1bxy' size='340' side='right'caption='[[1bxy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bxy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bxy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPL30 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=1bxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxy OCA], [https://pdbe.org/1bxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxy RCSB], [https://www.ebi.ac.uk/pdbsum/1bxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxy ProSAT]</span></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=1bxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxy OCA], [https://pdbe.org/1bxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxy RCSB], [https://www.ebi.ac.uk/pdbsum/1bxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RL30_THETH RL30_THETH]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1bxy ConSurf].
</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=1bxy ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of ribosomal protein L30 from the extreme thermophilic bacterium Thermus thermophilus has been determined at 1. 9 A resolution. The crystals are trigonal and belong to space group P3(2)21, with unit-cell parameters a = b = 63.5, c = 77.8 A, alpha = beta = 90, gamma = 120 degrees and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with X-PLOR to an R value of 20.3% and an R(free) of 25.3% in the resolution range 8-1.9 A. Detailed analyses of the structures of the two molecules in the asymmetric unit and comparison of T. thermophilus L30 structure with the structure of homologous L30 from Bacillus stearothermophilus reveal two flexible regions at opposite ends of the rather elongated molecule. Such flexibility could be important for the protein fitting in the ribosome. A comparison with B. stearothermophilus L30 shows a higher number of salt bridges and unbound positively charged residues and an increased accessible hydrophobic area on the surface of T. thermophilus L30. This could contribute to the stability of both the extreme thermophile protein and the ribosome as a whole.
Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.,Fedorov R, Nevskaya N, Khairullina A, Tishchenko S, Mikhailov A, Garber M, Nikonov S Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1827-33. PMID:10531479<ref>PMID:10531479</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bxy" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L30|Ribosomal protein L30]]
*[[Ribosomal protein L30|Ribosomal protein L30]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fedorov, R]]
[[Category: Thermus thermophilus]]
[[Category: Garber, M]]
[[Category: Fedorov R]]
[[Category: Khairullina, A]]
[[Category: Garber M]]
[[Category: Mikhailov, A]]
[[Category: Khairullina A]]
[[Category: Nevskaya, N]]
[[Category: Mikhailov A]]
[[Category: Nikonov, S]]
[[Category: Nevskaya N]]
[[Category: Tishchenko, S]]
[[Category: Nikonov S]]
[[Category: Conformational change]]
[[Category: Tishchenko S]]
[[Category: Ribosomal protein]]
[[Category: Ribosome]]

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