2e1a: Difference between revisions

Revision as of 18:04, 21 February 2008

crystal structure of FFRP-DM1

OverviewOverview

Feast/famine regulatory proteins (FFRPs) comprise the largest group of archaeal transcription factors. Crystal structures of an FFRP, DM1 from Pyrococcus, were determined in complex with isoleucine, which increases the association state of DM1 to form octamers, and with selenomethionine, which decreases it to maintain dimers under some conditions. Asp39 and Thr/Ser at 69-71 were identified as being important for interaction with the ligand main chain. By analyzing residues surrounding the ligand side chain, partner ligands were identified for various FFRPs from Pyrococcus, e.g., lysine facilitates homo-octamerization of FL11, and arginine facilitates hetero-octamerization of FL11 and DM1. Transcription of the fl11 gene and lysine synthesis are regulated by shifting the equilibrium between association states of FL11 and by shifting the equilibrium toward association with DM1, in response to amino acid availability. With FFRPs also appearing in eubacteria, the origin of such regulation can be traced back to the common ancestor of all extant organisms, serving as a prototype of transcription regulations, now highly diverged.

About this StructureAbout this Structure

2E1A is a Single protein structure of sequence from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands., Okamura H, Yokoyama K, Koike H, Yamada M, Shimowasa A, Kabasawa M, Kawashima T, Suzuki M, Structure. 2007 Oct;15(10):1325-38. PMID:17937921

Page seeded by OCA on Thu Feb 21 17:04:47 2008

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OCA

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 ==Overview==
-Feast/famine regulatory proteins (FFRPs) comprise the largest group of, archaeal transcription factors. Crystal structures of an FFRP, DM1 from, Pyrococcus, were determined in complex with isoleucine, which increases, the association state of DM1 to form octamers, and with selenomethionine, which decreases it to maintain dimers under some conditions. Asp39 and, Thr/Ser at 69-71 were identified as being important for interaction with, the ligand main chain. By analyzing residues surrounding the ligand side, chain, partner ligands were identified for various FFRPs from Pyrococcus, e.g., lysine facilitates homo-octamerization of FL11, and arginine, facilitates hetero-octamerization of FL11 and DM1. Transcription of the, fl11 gene and lysine synthesis are regulated by shifting the equilibrium, between association states of FL11 and by shifting the equilibrium toward, association with DM1, in response to amino acid availability. With FFRPs, also appearing in eubacteria, the origin of such regulation can be traced, back to the common ancestor of all extant organisms, serving as a, prototype of transcription regulations, now highly diverged.
+Feast/famine regulatory proteins (FFRPs) comprise the largest group of archaeal transcription factors. Crystal structures of an FFRP, DM1 from Pyrococcus, were determined in complex with isoleucine, which increases the association state of DM1 to form octamers, and with selenomethionine, which decreases it to maintain dimers under some conditions. Asp39 and Thr/Ser at 69-71 were identified as being important for interaction with the ligand main chain. By analyzing residues surrounding the ligand side chain, partner ligands were identified for various FFRPs from Pyrococcus, e.g., lysine facilitates homo-octamerization of FL11, and arginine facilitates hetero-octamerization of FL11 and DM1. Transcription of the fl11 gene and lysine synthesis are regulated by shifting the equilibrium between association states of FL11 and by shifting the equilibrium toward association with DM1, in response to amino acid availability. With FFRPs also appearing in eubacteria, the origin of such regulation can be traced back to the common ancestor of all extant organisms, serving as a prototype of transcription regulations, now highly diverged.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-A Structural Code for Discriminating between Transcription Signals Revealed by the Feast/Famine Regulatory Protein DM1 in Complex with Ligands., Okamura H, Yokoyama K, Koike H, Yamada M, Shimowasa A, Kabasawa M, Kawashima T, Suzuki M, Structure. 2007 Oct 16;15(10):1325-1338. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17937921 17937921]
+A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands., Okamura H, Yokoyama K, Koike H, Yamada M, Shimowasa A, Kabasawa M, Kawashima T, Suzuki M, Structure. 2007 Oct;15(10):1325-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17937921 17937921]
 [[Category: Pyrococcus horikoshii]]
 [[Category: Single protein]]
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 [[Category: transcriptional regulatory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:31:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:47 2008''