4f9t: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4f9t]] is a 1 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=4F9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F9T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4f9t]] is a 1 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=4F9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F9T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.46&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4f9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f9t OCA], [https://pdbe.org/4f9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f9t RCSB], [https://www.ebi.ac.uk/pdbsum/4f9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f9t 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=4f9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f9t OCA], [https://pdbe.org/4f9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f9t RCSB], [https://www.ebi.ac.uk/pdbsum/4f9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f9t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/RL1_THETH RL1_THETH] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318]  Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
[https://www.uniprot.org/uniprot/RL1_THETH RL1_THETH] The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.[HAMAP-Rule:MF_01318]  Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nine mutant forms of ribosomal proteins L1 from the bacterium Thermus thermophilus and the archaeon Methanococcus jannaschii were obtained. Their crystal structures were determined and analyzed. Earlier determined structure of S179C TthL1 was also thoroughly analyzed. Five from ten mutant proteins reveal essential changes of spatial structure caused by surface point mutation. It proves that for correct studies of biological processes by site-directed mutagenesis it is necessary to determine or at least to model spatial structures of mutant proteins. Detailed comparison of mutant L1 structures with that of corresponding wild type proteins reveals that side chain of a mutated amino acid residue tries to locate like the side chain of the original residue in the wild type protein. This observation helps to model the mutant structures.
[Crystal structures of mutant ribosomal proteins L1].,Nikonova EIu, Volchkov SA, Kliashtornyi VG, Tishchenko SV, Kostareva OS, Nevskaia NA, Nikonov OS, Gabdulkhakov AG, Nikulin AD, Davydova NL, Strel'tsov VA, Garber MB, Nikonov SV Mol Biol (Mosk). 2007 Jul-Aug;41(4):688-96. PMID:17936990<ref>PMID:17936990</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4f9t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L1|Ribosomal protein L1]]
*[[Ribosomal protein L1|Ribosomal protein L1]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 11:13, 1 March 2024

Ribosomal protein L1 from Thermus thermophilus with substitution Thr217Ala

4f9t, resolution 1.46Å

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