1c04: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c04]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C04 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c04]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C04 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rl2|1rl2]], [[1rl6|1rl6]], [[1whi|1whi]], [[430d|430d]], [[1qa6|1qa6]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1c04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c04 OCA], [https://pdbe.org/1c04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c04 RCSB], [https://www.ebi.ac.uk/pdbsum/1c04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c04 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=1c04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c04 OCA], [https://pdbe.org/1c04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c04 RCSB], [https://www.ebi.ac.uk/pdbsum/1c04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c04 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RL14_GEOSE RL14_GEOSE]] Forms part of two intersubunit bridges in the 70S ribosome (By similarity). Binds to 23S rRNA. [[https://www.uniprot.org/uniprot/RL6_GEOSE RL6_GEOSE]] It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center (By similarity). This protein binds to the 23S rRNA, and is important in its secondary structure.[HAMAP-Rule:MF_01365] [[https://www.uniprot.org/uniprot/RL2_GEOSE RL2_GEOSE]] One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (By similarity).[HAMAP-Rule:MF_01320] [[https://www.uniprot.org/uniprot/RL11_GEOSE RL11_GEOSE]] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
[https://www.uniprot.org/uniprot/RL2_GEOSE RL2_GEOSE] One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (By similarity).[HAMAP-Rule:MF_01320]
== 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=1c04 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=1c04 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have calculated at 5.0 A resolution an electron-density map of the large 50S ribosomal subunit from the bacterium Haloarcula marismortui by using phases derived from four heavy-atom derivatives, intercrystal density averaging and density-modification procedures. More than 300 base pairs of A-form RNA duplex have been fitted into this map, as have regions of non-A-form duplex, single-stranded segments and tetraloops. The long rods of RNA crisscrossing the subunit arise from the stacking of short, separate double helices, not all of which are A-form, and in many places proteins crosslink two or more of these rods. The polypeptide exit channel was marked by tungsten cluster compounds bound in one heavy-atom-derivatized crystal. We have determined the structure of the translation-factor-binding centre by fitting the crystal structures of the ribosomal proteins L6, L11 and L14, the sarcin-ricin loop RNA, and the RNA sequence that binds L11 into the electron density. We can position either elongation factor G or elongation factor Tu complexed with an aminoacylated transfer RNA and GTP onto the factor-binding centre in a manner that is consistent with results from biochemical and electron microscopy studies.
Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit.,Ban N, Nissen P, Hansen J, Capel M, Moore PB, Steitz TA Nature. 1999 Aug 26;400(6747):841-7. PMID:10476961<ref>PMID:10476961</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1c04" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L11|Ribosomal protein L11]]
*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
*[[Ribosomal protein L14|Ribosomal protein L14]]
*[[Ribosomal protein L14|Ribosomal protein L14]]
*[[Ribosomal protein L2|Ribosomal protein L2]]
*[[Ribosomal protein L2|Ribosomal protein L2]]
*[[Ribosomal protein L6|Ribosomal protein L6]]
*[[Ribosomal protein L6|Ribosomal protein L6]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ban, N]]
[[Category: Ban N]]
[[Category: Capel, M]]
[[Category: Capel M]]
[[Category: Moore, P B]]
[[Category: Moore PB]]
[[Category: Nissen, P]]
[[Category: Nissen P]]
[[Category: Steitz, T A]]
[[Category: Steitz TA]]
[[Category: Large ribosome unit]]
[[Category: Low resolution model]]
[[Category: Ribosome]]
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