1a32: Difference between revisions

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<StructureSection load='1a32' size='340' side='right'caption='[[1a32]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1a32' size='340' side='right'caption='[[1a32]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a32]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A32 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=1a32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a32 OCA], [http://pdbe.org/1a32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a32 RCSB], [http://www.ebi.ac.uk/pdbsum/1a32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a32 ProSAT]</span></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]] 2.1&#8491;</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=1a32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a32 OCA], [https://pdbe.org/1a32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a32 RCSB], [https://www.ebi.ac.uk/pdbsum/1a32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RS15_GEOSE RS15_GEOSE]] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (By similarity).[HAMAP-Rule:MF_01343]  Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome (By similarity).[HAMAP-Rule:MF_01343]  
[https://www.uniprot.org/uniprot/RS15_GEOSE RS15_GEOSE] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (By similarity).[HAMAP-Rule:MF_01343]  Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome (By similarity).[HAMAP-Rule:MF_01343]
== 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=1a32 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=1a32 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Ribosomal protein S15 is a primary RNA-binding protein that binds to the central domain of 16S rRNA. S15 also regulates its own synthesis by binding to its own mRNA. The binding sites for S15 on both mRNA and rRNA have been narrowed down to less than a hundred nucleotides each, making the protein an attractive candidate for the study of protein-RNA interactions. RESULTS: The crystal structure of S15 from Bacillus stearothermophilus has been solved to 2.1 A resolution. The structure consists of four alpha helices. Three of these helices form the core of the protein, while the N-terminal helix protrudes out from the body of the molecule to make contacts with a neighboring molecule in the crystal lattice. S15 contains a large conserved patch of basic residues which could provide a site for binding 16S rRNA. CONCLUSIONS: The conformation of the N-terminal alpha helix is quite different from that reported in a recent NMR structure of S15 from Thermus thermophilus. The intermolecular contacts that this alpha helix makes with a neighboring molecule in the crystal, however, closely resemble the intramolecular contacts that occur in the NMR structure. This conformational variability of the N-terminal helix has implications for the range of possible S15-RNA interactions. A large, conserved basic patch at one end of S15 and a cluster of conserved but exposed aromatic residues at the other end provide two possible RNA-binding sites on S15.
Conformational variability of the N-terminal helix in the structure of ribosomal protein S15.,Clemons WM Jr, Davies C, White SW, Ramakrishnan V Structure. 1998 Apr 15;6(4):429-38. PMID:9562554<ref>PMID:9562554</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a32" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein S15|Ribosomal protein S15]]
*[[Ribosomal protein S15|Ribosomal protein S15]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davies, C]]
[[Category: Clemons Junior WM]]
[[Category: Junior, W M.Clemons]]
[[Category: Davies C]]
[[Category: Ramakrishnan, V]]
[[Category: Ramakrishnan V]]
[[Category: White, S W]]
[[Category: White SW]]
[[Category: Multiwavelength anomalous diffraction]]
[[Category: Protein-rna]]
[[Category: Ribosomal protein]]
[[Category: Ribosomal protein interaction]]
[[Category: Ribosome]]
[[Category: Rna-binding]]

Latest revision as of 09:27, 7 February 2024

RIBOSOMAL PROTEIN S15 FROM BACILLUS STEAROTHERMOPHILUSRIBOSOMAL PROTEIN S15 FROM BACILLUS STEAROTHERMOPHILUS

Structural highlights

1a32 is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RS15_GEOSE One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (By similarity).[HAMAP-Rule:MF_01343] Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome (By similarity).[HAMAP-Rule:MF_01343]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1a32, resolution 2.10Å

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