1i1g: Difference between revisions

Revision as of 14:07, 21 February 2008

CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS

OverviewOverview

The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 A resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta-sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.

About this StructureAbout this Structure

1I1G is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus., Leonard PM, Smits SH, Sedelnikova SE, Brinkman AB, de Vos WM, van der Oost J, Rice DW, Rafferty JB, EMBO J. 2001 Mar 1;20(5):990-7. PMID:11230123

Page seeded by OCA on Thu Feb 21 13:07:00 2008

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OCA

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-[[Image:1i1g.gif|left|200px]]<br /><applet load="1i1g" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i1g.gif|left|200px]]<br /><applet load="1i1g" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i1g, resolution 2.9&Aring;" />
 '''CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS'''<br />
 ==Overview==
-The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus, belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of, which the Escherichia coli leucine-responsive regulatory protein is the, archetype. Its crystal structure has been determined at 2.9 A resolution, and is the first for a member of the Lrp/AsnC family, as well as one of, the first for a transcriptional regulator from a hyperthermophile. The, structure consists of an N-terminal domain containing a helix-turn-helix, (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta, character reminiscent of a number of RNA- and DNA-binding domains., Pyrococcus furiosus LrpA forms a homodimer mainly through interactions, between the antiparallel beta-sheets of the C-terminal domain, and further, interactions lead to octamer formation. The LrpA structure suggests how, the protein might bind and possibly distort its DNA substrate through use, of its HtH motifs and control gene expression. A possible location for an, effector binding site is proposed by using sequence comparisons with other, members of the family coupled to mutational analysis.
+The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 A resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta-sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.
 ==About this Structure==
-I1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I1G OCA].
+I1G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1G OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Pyrococcus furiosus]]
 [[Category: Single protein]]
-[[Category: Brinkman, A.B.]]
+[[Category: Brinkman, A B.]]
-[[Category: Leonard, P.M.]]
+[[Category: Leonard, P M.]]
-[[Category: Oost, J.van.der.]]
+[[Category: Oost, J van der.]]
-[[Category: Rafferty, J.B.]]
+[[Category: Rafferty, J B.]]
-[[Category: Rice, D.W.]]
+[[Category: Rice, D W.]]
-[[Category: Sedelnikova, S.E.]]
+[[Category: Sedelnikova, S E.]]
-[[Category: Smits, S.H.J.]]
+[[Category: Smits, S H.J.]]
-[[Category: Vos, W.M.de.]]
+[[Category: Vos, W M.de.]]
 [[Category: helix-turn-helix]]
 [[Category: lrp/asnc family]]
@@ Line 26: / Line 26: @@
 [[Category: transcriptional regulator]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:58:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:00 2008''