1RI7
crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3
Summary for 1RI7
| Entry DOI | 10.2210/pdb1ri7/pdb |
| Descriptor | Putative transcriptional regulator (2 entities in total) |
| Functional Keywords | lrp/asnc family, transcription, dna binding protein |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 1 |
| Total formula weight | 19151.22 |
| Authors | Koike, H.,Suzuki, M. (deposition date: 2003-11-16, release date: 2004-03-09, Last modification date: 2024-03-13) |
| Primary citation | Koike, H.,Ishijima, S.A.,Clowney, L.,Suzuki, M. The archaeal feast/famine regulatory protein: Potential roles of its assembly forms for regulating transcription Proc.Natl.Acad.Sci.USA, 101:2840-2845, 2004 Cited by PubMed Abstract: The 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. PubMed: 14976242DOI: 10.1073/pnas.0400109101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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