1ri7
crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3
Structural highlights
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 PubMedThe classification feast/famine regulatory proteins (FFRPs) encompasses archaeal DNA-binding proteins with Escherichia coli transcription factors, the leucine-responsive regulatory protein and the asparagine synthase C gene product. In this paper, we describe two forms of the archaeal FFRP FL11 (pot0434017), both assembled from dimers. When crystallized, a helical cylinder is formed with six dimers per turn. In contrast, in solution, disks are formed, most likely consisting of four dimers each; an observation by cryoelectron microscopy. Whereas each dimer binds a 13-bp sequence, different forms will discriminate between promoters, based on the numbers of repeating 13-bp sequences, and types of linkers inserted between them, which are either of 7-8 or approximately 18 bp. The amino acid sequences of these FFRPs are designed to form the same type of 3D structures, and the transition between their assembly forms is regulated by interaction with small molecules. These considerations lead us to propose a possible mechanism for regulating a number of genes by varying assembly forms and by combining different FFRPs into these assemblies, responding to environmental changes. The archaeal feast/famine regulatory protein: potential roles of its assembly forms for regulating transcription.,Koike H, Ishijima SA, Clowney L, Suzuki M Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2840-5. Epub 2004 Feb 19. PMID:14976242[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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