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1n88

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Revision as of 10:06, 25 October 2017

NMR structure of the ribosomal protein L23 from Thermus thermophilus.

Structural highlights

1n88 is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL23_THETH] One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome (By similarity).

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 PubMed

The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed.

NMR structure of the ribosomal protein L23 from Thermus thermophilus.,Ohman A, Rak A, Dontsova M, Garber MB, Hard T J Biomol NMR. 2003 Jun;26(2):131-7. PMID:12766408^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ohman A, Rak A, Dontsova M, Garber MB, Hard T. NMR structure of the ribosomal protein L23 from Thermus thermophilus. J Biomol NMR. 2003 Jun;26(2):131-7. PMID:12766408

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n88"

@@ Line 1: / Line 1: @@
 ==NMR structure of the ribosomal protein L23 from Thermus thermophilus.==
 <StructureSection load='1n88' size='340' side='right' caption='[[1n88]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1n88]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N88 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N88 FirstGlance]. <br>
-</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=1n88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n88 OCA], [http://pdbe.org/1n88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n88 RCSB], [http://www.ebi.ac.uk/pdbsum/1n88 PDBsum]</span></td></tr>
+</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=1n88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n88 OCA], [http://pdbe.org/1n88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n88 RCSB], [http://www.ebi.ac.uk/pdbsum/1n88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n88 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
     <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/chain_selection.php?pdb_ID=2ata 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=1n88 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 </div>
 <div class="pdbe-citations 1n88" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ribosomal protein L23|Ribosomal protein L23]]
 == References ==
 <references/>

1n88

From Proteopedia

Revision as of 10:06, 25 October 2017

NMR structure of the ribosomal protein L23 from Thermus thermophilus.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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