1ck2: Difference between revisions

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<StructureSection load='1ck2' size='340' side='right'caption='[[1ck2]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1ck2' size='340' side='right'caption='[[1ck2]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ck2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CK2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ck2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CK2 FirstGlance]. <br>
</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=1ck2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck2 OCA], [https://pdbe.org/1ck2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ck2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ck2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ck2 ProSAT]</span></td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPL30 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1ck2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck2 OCA], [https://pdbe.org/1ck2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ck2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ck2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ck2 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mao, H]]
[[Category: Mao, H]]

Revision as of 13:32, 16 February 2022

YEAST (SACCHAROMYCES CEREVISIAE) RIBOSOMAL PROTEIN L30YEAST (SACCHAROMYCES CEREVISIAE) RIBOSOMAL PROTEIN L30

Structural highlights

1ck2 is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:RPL30 (ATCC 18824)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 L30 from yeast Saccharomyces cerevisiae auto-regulates its own synthesis by binding to a structural element in both its pre-mRNA and its mRNA. The three-dimensional structures of L30 in the free (f L30) and the pre-mRNA bound (b L30) forms have been solved by nuclear magnetic resonance spectroscopy. Both protein structures contain four alternating alpha-helices and four beta-strands segments and adopt an overall topology that is an alphabetaalpha three-layer sandwich, representing a unique fold. Three loops on one end of the alphabetaalpha sandwich have been mapped as the RNA binding site on the basis of structural comparison, chemical shift perturbation and the inter-molecular nuclear Overhauser effects to the RNA. The structural and dynamic comparison of f L30 and b L30 reveals that local dynamics may play an important role in the RNA binding. The fourth helix in b L30 is longer than in f L30, and is stabilized by RNA binding. The exposed hydrophobic surface that is buried upon RNA binding may provide the energy necessary to drive secondary structure formation, and may account for the increased stability of b L30.

Local folding coupled to RNA binding in the yeast ribosomal protein L30.,Mao H, Williamson JR J Mol Biol. 1999 Sep 17;292(2):345-59. PMID:10493880[1]

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

See Also

References

  1. Mao H, Williamson JR. Local folding coupled to RNA binding in the yeast ribosomal protein L30. J Mol Biol. 1999 Sep 17;292(2):345-59. PMID:10493880 doi:10.1006/jmbi.1999.3044
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