1mms: Difference between revisions
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<StructureSection load='1mms' size='340' side='right'caption='[[1mms]], [[Resolution|resolution]] 2.57Å' scene=''> | <StructureSection load='1mms' size='340' side='right'caption='[[1mms]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mms]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1mms]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MMC:METHYL+MERCURY+ION'>MMC</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]] 2.57Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MMC:METHYL+MERCURY+ION'>MMC</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=1mms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mms OCA], [https://pdbe.org/1mms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mms RCSB], [https://www.ebi.ac.uk/pdbsum/1mms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mms 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=1mms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mms OCA], [https://pdbe.org/1mms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mms RCSB], [https://www.ebi.ac.uk/pdbsum/1mms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mms ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA] This protein binds directly to 23S ribosomal RNA. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Ribosomal protein L11|Ribosomal protein L11]] | *[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Guymon | [[Category: Thermotoga maritima]] | ||
[[Category: Mccutcheon | [[Category: Guymon R]] | ||
[[Category: Ramakrishnan | [[Category: Mccutcheon JP]] | ||
[[Category: White | [[Category: Ramakrishnan V]] | ||
[[Category: Wimberly | [[Category: White SW]] | ||
[[Category: Wimberly BT]] | |||
Latest revision as of 02:43, 28 December 2023
Crystal structure of the ribosomal PROTEIN L11-RNA complexCrystal structure of the ribosomal PROTEIN L11-RNA complex
Structural highlights
FunctionRL11_THEMA This protein binds directly to 23S ribosomal RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors. A detailed view of a ribosomal active site: the structure of the L11-RNA complex.,Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V Cell. 1999 May 14;97(4):491-502. PMID:10338213[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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