1qd7: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT== | |||
<StructureSection load='1qd7' size='340' side='right'caption='[[1qd7]], [[Resolution|resolution]] 5.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1qd7]] is a 10 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=1QD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QD7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N:ANY+5-MONOPHOSPHATE+NUCLEOTIDE'>N</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=1qd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd7 OCA], [https://pdbe.org/1qd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qd7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qd7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RS4_GEOSE RS4_GEOSE] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (By similarity).[HAMAP-Rule:MF_01306_B] With S5 and S12 plays an important role in translational accuracy (By similarity).[HAMAP-Rule:MF_01306_B] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qd7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1qd7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 30S ribosomal subunit binds messenger RNA and the anticodon stem-loop of transfer RNA during protein synthesis. A crystallographic analysis of the structure of the subunit from the bacterium Thermus thermophilus is presented. At a resolution of 5.5 A, the phosphate backbone of the ribosomal RNA is visible, as are the alpha-helices of the ribosomal proteins, enabling double-helical regions of RNA to be identified throughout the subunit, all seven of the small-subunit proteins of known crystal structure to be positioned in the electron density map, and the fold of the entire central domain of the small-subunit ribosomal RNA to be determined. | |||
Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution.,Clemons WM Jr, May JL, Wimberly BT, McCutcheon JP, Capel MS, Ramakrishnan V Nature. 1999 Aug 26;400(6747):833-40. PMID:10476960<ref>PMID:10476960</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1qd7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 18: | Line 38: | ||
*[[Ribosomal protein S7|Ribosomal protein S7]] | *[[Ribosomal protein S7|Ribosomal protein S7]] | ||
*[[Ribosomal protein S8|Ribosomal protein S8]] | *[[Ribosomal protein S8|Ribosomal protein S8]] | ||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Capel | [[Category: Capel MS]] | ||
[[Category: Clemons | [[Category: Clemons Jr WM]] | ||
[[Category: May | [[Category: May JLC]] | ||
[[Category: McCutcheon | [[Category: McCutcheon JP]] | ||
[[Category: Ramakrishnan | [[Category: Ramakrishnan V]] | ||
[[Category: Wimberly | [[Category: Wimberly BT]] | ||
Latest revision as of 13:01, 16 August 2023
PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNITPARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT
Structural highlights
FunctionRS4_GEOSE One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (By similarity).[HAMAP-Rule:MF_01306_B] With S5 and S12 plays an important role in translational accuracy (By similarity).[HAMAP-Rule:MF_01306_B] 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 PubMedThe 30S ribosomal subunit binds messenger RNA and the anticodon stem-loop of transfer RNA during protein synthesis. A crystallographic analysis of the structure of the subunit from the bacterium Thermus thermophilus is presented. At a resolution of 5.5 A, the phosphate backbone of the ribosomal RNA is visible, as are the alpha-helices of the ribosomal proteins, enabling double-helical regions of RNA to be identified throughout the subunit, all seven of the small-subunit proteins of known crystal structure to be positioned in the electron density map, and the fold of the entire central domain of the small-subunit ribosomal RNA to be determined. Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution.,Clemons WM Jr, May JL, Wimberly BT, McCutcheon JP, Capel MS, Ramakrishnan V Nature. 1999 Aug 26;400(6747):833-40. PMID:10476960[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
|
| ||||||||||||||||||