1reg

CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1reg, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1reg is a 2 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [REGA_BPT4] Controls the translation of a number of proteins (such as regA itself, rIIB and at least 35 others) by binding to their mRNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction. Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution.,Kang C, Chan R, Berger I, Lockshin C, Green L, Gold L, Rich A Science. 1995 May 26;268(5214):1170-3. PMID:7761833 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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