1fow

From Proteopedia

(Difference between revisions)

Revision as of 11:12, 28 July 2021

NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1fow is a 1 chain structure with sequence from Atcc 12980. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1fox
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL11_GEOSE] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.

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 structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.

High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA.,Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA Nat Struct Biol. 1997 Jan;4(1):70-7. PMID:8989327^[1]

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

References

↑ Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. Nat Struct Biol. 1997 Jan;4(1):70-7. PMID:8989327

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1fow' size='340' side='right'caption='[[1fow]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fow]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FOW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fow]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOW FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fox|1fox]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fox|1fox]]</div></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=1fow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fow OCA], [http://pdbe.org/1fow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fow RCSB], [http://www.ebi.ac.uk/pdbsum/1fow PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fow 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=1fow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fow OCA], [https://pdbe.org/1fow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fow RCSB], [https://www.ebi.ac.uk/pdbsum/1fow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fow ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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/RL11_GEOSE RL11_GEOSE]] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fow

From Proteopedia

Revision as of 11:12, 28 July 2021

NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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