3cc2

From Proteopedia

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Revision as of 10:18, 10 January 2011

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Template:STRUCTURE 3cc2

Contents 1 The Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution with rrnA Sequence for the 23S rRNA and Genome-derived Sequences for r-Proteins 2 About this Structure 3 See Also 4 Reference

The Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution with rrnA Sequence for the 23S rRNA and Genome-derived Sequences for r-Proteins

Template:ABSTRACT PUBMED 18455733

About this Structure

3cc2 is a 30 chain structure of Ribosomal protein L10, Ribosomal protein L2, Ribosomal protein L3, Ribosomal protein L4, Ribosomal protein L5, Ribosomal protein L6, Ribosomal protein L7 and Ribosome with sequence from Haloarcula marismortui. Full crystallographic information is available from OCA.

See Also

• Jmol/Visualizing large molecules
• Large Ribosomal Subunit of Haloarcula
• Ribosomal protein L10
• Ribosomal protein L2
• Ribosomal protein L3
• Ribosomal protein L4
• Ribosomal protein L5
• Ribosomal protein L6
• Ribosomal protein L7
• Ribosome
• User:Wayne Decatur/Haloarcula Large Ribosomal Subunit
• User:Wayne Decatur/Haloarcula Large Ribosomal Subunit With Azithromycin
• User:Wayne Decatur/kink-turn motif

Reference

• Blaha G, Gurel G, Schroeder SJ, Moore PB, Steitz TA. Mutations outside the anisomycin-binding site can make ribosomes drug-resistant. J Mol Biol. 2008 Jun 6;379(3):505-19. Epub 2008 Apr 8. PMID:18455733 doi:http://dx.doi.org/10.1016/j.jmb.2008.03.075
• Klein DJ, Moore PB, Steitz TA. The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J Mol Biol. 2004 Jun 25;340(1):141-77. PMID:15184028 doi:10.1016/j.jmb.2004.03.076
• Baliga NS, Bonneau R, Facciotti MT, Pan M, Glusman G, Deutsch EW, Shannon P, Chiu Y, Weng RS, Gan RR, Hung P, Date SV, Marcotte E, Hood L, Ng WV. Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea. Genome Res. 2004 Nov;14(11):2221-34. PMID:15520287 doi:14/11/2221