1ri7
From Proteopedia
(New page: 200px<br /><applet load="1ri7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ri7, resolution 2.7Å" /> '''crystal structure of ...) |
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| - | [[Image:1ri7.jpg|left|200px]]<br /><applet load="1ri7" size=" | + | [[Image:1ri7.jpg|left|200px]]<br /><applet load="1ri7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ri7, resolution 2.7Å" /> | caption="1ri7, resolution 2.7Å" /> | ||
'''crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3'''<br /> | '''crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The classification feast/famine regulatory proteins (FFRPs) encompasses | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1RI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_sp. Paracoccus sp.]. Full crystallographic information is available from [http:// | + | 1RI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_sp. Paracoccus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:09 2008'' |
Revision as of 12:51, 21 February 2008
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crystal structure of a protein in the LRP/ASNC family from the hyperthermophilic archaeon Pyrococcus sp. OT3
Overview
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.
About this Structure
1RI7 is a Single protein structure of sequence from Paracoccus sp.. Full crystallographic information is available from OCA.
Reference
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
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