NDLI: A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study

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A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study

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A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gaitatzes, C. G. Smith, T. F. Hisbergues, M. Joset, F. Bedu, S.
Description	Country affiliation: France Author Affiliation: Hisbergues M ( Laboratoire de Chimie bacterienne--Centre National de la Recherche Scientifique, F13402 Marseilles Cedex 20, France.)
Abstract	SYNECHOCYSTIS: PCC6803 possesses several open reading frames encoding putative WD-repeat proteins. One, the Hat protein, is involved in the control of a high-affinity transport system for inorganic carbon that is active when the cells are grown under a limiting concentration of this carbon substrate. The protein is composed of two major domains separated by a hydrophobic linker region of 20 amino acid residues. The N-terminal domain of Hat has no homolog in standard databases and does not display any particular structural features. Eleven WD repeats have been identified in the C-terminal moiety. The region encompassing the four terminal WD repeats is essential for growth under a limiting inorganic carbon regime. The region encompassing the two most terminal WD repeats is required for the activity of the high-affinity transport system. However, because the Hat protein is located in the thylakoids, it should not be itself an element of the transport system. The structural organization of the WD-containing domain of Hat was modeled from the crystal structure of the G protein beta subunit (with seven WD repeats) and of hemopexin (a structural analog with four blades). Functional and structural data argue in favor of an organization of the Hat WD moiety in two subdomains of seven and four WD repeats. The C-terminal 4-mer subdomain might interact with another, yet unknown, protein/peptide. This interaction could be essential in modulating the stability of the 4-mer structure and, thus, the accessibility of this subdomain, or at least of the region encompassing the last two WD repeats.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	2
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cyanobacteria Chemistry Membrane Transport Proteins Amino Acid Sequence Bacterial Proteins Genetics Pharmacokinetics Crystallography, X-ray Gene Deletion Hemopexin Models, Molecular Molecular Sequence Data Mutagenesis Mutagenesis, Site-directed Open Reading Frames Peptides Phenotype Phosphorylation Protein Structure, Tertiary Sequence Homology, Amino Acid Structure-activity Relationship Subcellular Fractions Thylakoids Time Factors Transcription Factors Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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