2dog

<StructureSection load='2dog' size='340' side='right' caption='[[2dog]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2dog]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DOG FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rimM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=2dog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dog OCA], [http://pdbe.org/2dog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dog RCSB], [http://www.ebi.ac.uk/pdbsum/2dog PDBsum], [http://www.topsan.org/Proteins/RSGI/2dog TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/RIMM_THET8 RIMM_THET8]] An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/2dog_consurf.spt"</scriptWhenChecked>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:17616598</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2dog" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Thet8]]

[[Category: Kaminishi, T]]

[[Category: Kawazoe, M]]

[[Category: Matsumoto, E]]

[[Category: Muto, Y]]

[[Category: Structural genomic]]

[[Category: Shirouzu, M]]

[[Category: Suzuki, S]]

[[Category: Takemoto, C]]

[[Category: Tatsuguchi, A]]

[[Category: Yokoyama, S]]

[[Category: Unknown function]]