1dcj: Difference between revisions

Revision as of 13:15, 21 February 2008

SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION

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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OCA

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 '''SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION'''<br />
 ==Overview==
-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.
+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 Structure==
-DCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA].
+DCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA].
 ==Reference==
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 [[Category: structural genomics]]
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