1dmg

<table><tr><td colspan='2'>[[1dmg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DMG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></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=1dmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmg OCA], [http://pdbe.org/1dmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dmg RCSB], [http://www.ebi.ac.uk/pdbsum/1dmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmg ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RL4_THEMA RL4_THEMA]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).[HAMAP-Rule:MF_01328_B] This protein only weakly controls expression of the E.coli S10 operon. It is incorporated into E.coli ribosomes, however it is not as firmly associated as the endogenous protein.[HAMAP-Rule:MF_01328_B] Forms part of the polypeptide exit tunnel (By similarity).[HAMAP-Rule:MF_01328_B]

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== Publication Abstract from PubMed ==

Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon. The crystal structure of L4 from Thermotoga maritima at 1.7 A resolution shows the protein with an alternating alpha/beta fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking alpha-helices. The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive alpha-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.

Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon.,Worbs M, Huber R, Wahl MC EMBO J. 2000 Mar 1;19(5):807-18. PMID:10698923<ref>PMID:10698923</ref>

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

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== References ==

<references/>

[[Category: Huber, R]]

[[Category: Wahl, M C]]

[[Category: Worbs, M]]

[[Category: Alpha-beta]]

[[Category: S10 operon]]