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1bxy

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(New page: 200px<br /><applet load="1bxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxy, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1bxy.gif|left|200px]]<br /><applet load="1bxy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bxy, resolution 1.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.==
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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.
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<StructureSection load='1bxy' size='340' side='right'caption='[[1bxy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 1.9&#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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL30_THETH RL30_THETH]
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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/bx/1bxy_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=1bxy 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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1BXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BXY OCA].
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*[[Ribosomal protein L30|Ribosomal protein L30]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10531479 10531479]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Fedorov, R.]]
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[[Category: Fedorov R]]
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[[Category: Garber, M.]]
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[[Category: Garber M]]
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[[Category: Khairullina, A.]]
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[[Category: Khairullina A]]
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[[Category: Mikhailov, A.]]
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[[Category: Mikhailov A]]
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[[Category: Nevskaya, N.]]
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[[Category: Nevskaya N]]
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[[Category: Nikonov, S.]]
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[[Category: Nikonov S]]
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[[Category: Tishchenko, S.]]
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[[Category: Tishchenko S]]
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[[Category: conformational changes]]
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[[Category: ribosomal protein]]
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[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:00:46 2007''
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Current revision

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

PDB ID 1bxy

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