1dcj
SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION
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OverviewOverview
YhhP, a small protein of 81 amino acid residues encoded by the yhhP gene, in the Escherichia coli database, is implicated in cell division although, the precise biological function of this protein has not been yet, identified. A variety of microorganisms have similar proteins, all of, which contain a common CPxP sequence motif in the N-terminal region. We, have determined the three-dimensional solution structure of YhhP by NMR, spectroscopy in order to obtain insight into its biological function. It, folds into a two-layered alpha/beta-sandwich structure with a, betaalphabetaalphabetabeta fold, comprising a mixed four-stranded, beta-sheet stacked against two alpha-helices, both of which are nearly, parallel to the strands of the beta-sheet. The CPxP motif plays a, significant structural role in stabilizing the first helix as a part of, the new type N-capping box where the Cys-Pro peptide bond adopts a cis, configuration. The structure of YhhP displays a striking resemblance to, the C-terminal ribosome-binding domain of translation initiation factor, IF3 (IF3C). In addition, the surface charge distribution of the, RNA-recognition helix of IF3C is nearly the same as that of the, corresponding helix of YhhP. These results suggest a structure-based, hypothesis in which binding to an RNA target plays an essential role in, the function of this ubiquitous protein.
About this StructureAbout this Structure
1DCJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division., Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T, J Mol Biol. 2000 Nov 24;304(2):219-29. PMID:11080457
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