2dog
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The RimM protein has been implicated in the maturation of the 30S | + | The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Matsumoto, E.]] | [[Category: Matsumoto, E.]] | ||
[[Category: Muto, Y.]] | [[Category: Muto, Y.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Suzuki, S.]] | [[Category: Suzuki, S.]] | ||
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[[Category: unknown function]] | [[Category: unknown function]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:00:58 2008'' |
Revision as of 15:01, 21 February 2008
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Solution structure of the N-terminal domain of RimM from Thermus thermophilus HB8
Overview
The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19.
About this Structure
2DOG is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structural characterization of the ribosome maturation protein, RimM., Suzuki S, Tatsuguchi A, Matsumoto E, Kawazoe M, Kaminishi T, Shirouzu M, Muto Y, Takemoto C, Yokoyama S, J Bacteriol. 2007 Sep;189(17):6397-406. Epub 2007 Jul 6. PMID:17616598
Page seeded by OCA on Thu Feb 21 17:00:58 2008
Categories: Single protein | Thermus thermophilus | Kaminishi, T. | Kawazoe, M. | Matsumoto, E. | Muto, Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Suzuki, S. | Takemoto, C. | Tatsuguchi, A. | Yokoyama, S. | Beta barrel | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Unknown function
