2mmp: Difference between revisions
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<StructureSection load='2mmp' size='340' side='right'caption='[[2mmp]]' scene=''> | <StructureSection load='2mmp' size='340' side='right'caption='[[2mmp]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[2mmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMP 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=2mmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmp OCA], [https://pdbe.org/2mmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmp RCSB], [https://www.ebi.ac.uk/pdbsum/2mmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmp ProSAT]</span></td></tr> | </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=2mmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmp OCA], [https://pdbe.org/2mmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmp RCSB], [https://www.ebi.ac.uk/pdbsum/2mmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0KTR7_SACS9 D0KTR7_SACS9] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Three archaea-specific ribosomal proteins recently identified show no sequence homology with other known proteins. Here we determined the structure of L46a, the most conserved one among the three proteins, from Sulfolobus solfataricus P2 using NMR spectroscopy. The structure presents a twisted beta-sheet formed by the N-terminal part and two helices at the C-terminus. The L46a structure has a positively charged surface which is conserved in the L46a protein family and is the potential rRNA-binding site. Searching homologous structures in Protein Data Bank revealed that the structure of L46a represents a novel protein fold. The backbone dynamics identified by NMR relaxation experiments reveal significant flexibility at the rRNA binding surface. The potential position of L46a on the ribosome was proposed by fitting the structure into a previous electron microscopy map of the ribosomal 50S subunit, which indicated that L46a contacts to domain I of 23S rRNA near a multifunctional ribosomal protein L7ae. | |||
Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold.,Feng Y, Song X, Lin J, Xuan J, Cui Q, Wang J Biochem Biophys Res Commun. 2014 May 26. pii: S0006-291X(14)00949-8. doi:, 10.1016/j.bbrc.2014.05.077. PMID:24875358<ref>PMID:24875358</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mmp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Saccharolobus solfataricus P2]] | |||
[[Category: Feng Y]] | [[Category: Feng Y]] | ||
Revision as of 12:39, 14 June 2023
Solution structure of a ribosomal proteinSolution structure of a ribosomal protein
Structural highlights
FunctionPublication Abstract from PubMedThree archaea-specific ribosomal proteins recently identified show no sequence homology with other known proteins. Here we determined the structure of L46a, the most conserved one among the three proteins, from Sulfolobus solfataricus P2 using NMR spectroscopy. The structure presents a twisted beta-sheet formed by the N-terminal part and two helices at the C-terminus. The L46a structure has a positively charged surface which is conserved in the L46a protein family and is the potential rRNA-binding site. Searching homologous structures in Protein Data Bank revealed that the structure of L46a represents a novel protein fold. The backbone dynamics identified by NMR relaxation experiments reveal significant flexibility at the rRNA binding surface. The potential position of L46a on the ribosome was proposed by fitting the structure into a previous electron microscopy map of the ribosomal 50S subunit, which indicated that L46a contacts to domain I of 23S rRNA near a multifunctional ribosomal protein L7ae. Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold.,Feng Y, Song X, Lin J, Xuan J, Cui Q, Wang J Biochem Biophys Res Commun. 2014 May 26. pii: S0006-291X(14)00949-8. doi:, 10.1016/j.bbrc.2014.05.077. PMID:24875358[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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