1dcj: Difference between revisions
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[[Image:1dcj.gif|left|200px]] | [[Image:1dcj.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION''' | {{Structure | ||
|PDB= 1dcj |SIZE=350|CAPTION= <scene name='initialview01'>1dcj</scene> | |||
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'''SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DCJ is a [ | 1DCJ is a [[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== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11080457 11080457] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Yamazaki, T.]] | [[Category: Yamazaki, T.]] | ||
[[Category: alpha-beta sandwich]] | [[Category: alpha-beta sandwich]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:36:21 2008'' | ||
Revision as of 11:36, 20 March 2008
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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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