1imu

<StructureSection load='1imu' size='340' side='right'caption='[[1imu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1imu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IMU 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=1imu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imu OCA], [https://pdbe.org/1imu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1imu RCSB], [https://www.ebi.ac.uk/pdbsum/1imu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1imu ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RAIA_HAEIN RAIA_HAEIN]] During stationary phase, prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases. In addition, during environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation initiation and increase translation accuracy. When normal growth conditions are restored, is quickly released from the ribosome (By similarity).

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== Publication Abstract from PubMed ==

A novel bacterial ribosome binding protein, protein Y (also known as YfiA), was recently shown to reside at the 30S/50S subunit interface and to stabilize the ribosomal 70S complex against dissociation at low magnesium ion concentrations. We report here the three-dimensional NMR structure in solution of a homologue from Haemophilus influenzae, HI0257, that has 64% sequence identity to protein Y. The 107 residue protein has a beta-alpha-beta-beta-beta-alpha folding topology with two parallel alpha-helices packed against the same side of a four-stranded beta-sheet. The closest structural relatives are proteins with the double-stranded RNA-binding domain (dsRBD) motif although there is little (&lt;10%) sequence homology. The most immediate differences between the dsRBD and HI0257 structures are that (1) HI0257 has a larger beta-sheet motif with an extra beta-strand at the N-terminus, (2) the helices are parallel in HI0257 but at an angle of about 30 degrees to each other in the dsRBD, and (3) HI0257 lacks the extended loop commonly seen between the first and second beta-strands of the dsRBD. Further, an analysis of the surface electrostatic potential in HI0257 and the dsRBD family reveals significant differences in the location of contiguous positively (and negatively) charged regions. The structural data, in combination with sequence analysis of HI0257 and its homologues, suggest that the most likely mode of RNA recognition for HI0257 may be distinct from that of the dsRBD family of proteins.

Solution structure of HI0257, a bacterial ribosome binding protein.,Parsons L, Eisenstein E, Orban J Biochemistry. 2001 Sep 18;40(37):10979-86. PMID:11551193<ref>PMID:11551193</ref>

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

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<div class="pdbe-citations 1imu" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacterium influenzae lehmann and neumann 1896]]

[[Category: Eisenstein, E]]

[[Category: Orban, J]]

[[Category: Parsons, L]]

[[Category: Structure 2 function project]]