This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3j3w

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Atomic model of the immature 50S subunit from Bacillus subtilis (state II-a)

3j3w, resolution 10.70Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3j3w"

@@ Line 1: / Line 1: @@
 ==Atomic model of the immature 50S subunit from Bacillus subtilis (state II-a)==
-<StructureSection load='3j3w' size='340' side='right' caption='[[3j3w]], [[Resolution|resolution]] 10.70&Aring;' scene=''>
+<SX load='3j3w' size='340' side='right' viewer='molstar' caption='[[3j3w]], [[Resolution|resolution]] 10.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j3w]] is a 19 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J3W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j3w]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J3W FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j3v|3j3v]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10.7&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j3w RCSB], [http://www.ebi.ac.uk/pdbsum/3j3w PDBsum]</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=3j3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j3w OCA], [https://pdbe.org/3j3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j3w RCSB], [https://www.ebi.ac.uk/pdbsum/3j3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j3w ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/RL19_BACSU RL19_BACSU] This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site (By similarity).
-Ribosome assembly is a process fundamental for all cellular activities. The efficiency and accuracy of the subunit assembly are tightly regulated and closely monitored. In the present work, we characterized, both compositionally and structurally, a set of in vivo 50S subunit precursors (45S), isolated from a mutant bacterial strain. Our qualitative mass spectrometry data indicate that L28, L16, L33, L36 and L35 are dramatically underrepresented in the 45S particles. This protein spectrum shows interesting similarity to many qualitatively analyzed 50S precursors from different genetic background, indicating the presence of global rate-limiting steps in the late-stage assembly of 50S subunit. Our structural data reveal two major intermediate states for the 45S particles. Consistently, both states severally lack those proteins, but they also differ in the stability of the functional centers of the 50S subunit, demonstrating that they are translationally inactive. Detailed analysis indicates that the orientation of H38 accounts for the global conformational differences in these intermediate structures, and suggests that the reorientation of H38 to its native position is rate-limiting during the late-stage assembly. Especially, H38 plays an essential role in stabilizing the central protuberance, through the interaction with the 5S rRNA, and the correctly orientated H38 is likely a prerequisite for further maturation of the 50S subunit.
-Cryo-EM structures of the late-stage assembly intermediates of the bacterial 50S ribosomal subunit.,Li N, Chen Y, Guo Q, Zhang Y, Yuan Y, Ma C, Deng H, Lei J, Gao N Nucleic Acids Res. 2013 May 21. PMID:23700310<ref>PMID:23700310</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
 *[[Ribosome 3D structures|Ribosome 3D structures]]
-== References ==
-<references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Bacillus subtilis]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Gao, N]]
+[[Category: Large Structures]]
-[[Category: Guo, Q]]
+[[Category: Gao N]]
-[[Category: Lei, J]]
+[[Category: Guo Q]]
-[[Category: Li, N]]
+[[Category: Lei J]]
-[[Category: Ma, C]]
+[[Category: Li N]]
-[[Category: Yuan, Y]]
+[[Category: Ma C]]
-[[Category: Zhang, Y]]
+[[Category: Yuan Y]]
-[[Category: Ribosome]]
+[[Category: Zhang Y]]
-[[Category: Ribosome assembly]]
-[[Category: Ribosome biogenesis]]
-[[Category: Rna folding]]
-[[Category: Ylqf]]

3j3w

From Proteopedia

Current revision

Atomic model of the immature 50S subunit from Bacillus subtilis (state II-a)

Structural highlights

Function

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox