1f5m

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(New page: 200px<br /><applet load="1f5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f5m, resolution 1.9&Aring;" /> '''STRUCTURE OF THE GAF ...)
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caption="1f5m, resolution 1.9&Aring;" />
'''STRUCTURE OF THE GAF DOMAIN'''<br />
'''STRUCTURE OF THE GAF DOMAIN'''<br />
==Overview==
==Overview==
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GAF domains are ubiquitous motifs present in cyclic GMP (cGMP)-regulated, cyclic nucleotide phosphodiesterases, certain adenylyl cyclases, the, bacterial transcription factor FhlA, and hundreds of other signaling and, sensory proteins from all three kingdoms of life. The crystal structure of, the Saccharomyces cerevisiae YKG9 protein was determined at 1.9 A, resolution. The structure revealed a fold that resembles the PAS domain, another ubiquitous signaling and sensory transducer. YKG9 does not bind, cGMP, but the isolated first GAF domain of phosphodiesterase 5 binds with, K:(d) = 650 nM. The cGMP binding site of the phosphodiesterase GAF domain, was identified by homology modeling and site-directed mutagenesis, and, consists of conserved Arg, Asn, Lys and Asp residues. The structural and, binding studies taken together show that the cGMP binding GAF domains form, a new class of cyclic nucleotide receptors distinct from the regulatory, domains of cyclic nucleotide-regulated protein kinases and ion channels.
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GAF domains are ubiquitous motifs present in cyclic GMP (cGMP)-regulated cyclic nucleotide phosphodiesterases, certain adenylyl cyclases, the bacterial transcription factor FhlA, and hundreds of other signaling and sensory proteins from all three kingdoms of life. The crystal structure of the Saccharomyces cerevisiae YKG9 protein was determined at 1.9 A resolution. The structure revealed a fold that resembles the PAS domain, another ubiquitous signaling and sensory transducer. YKG9 does not bind cGMP, but the isolated first GAF domain of phosphodiesterase 5 binds with K:(d) = 650 nM. The cGMP binding site of the phosphodiesterase GAF domain was identified by homology modeling and site-directed mutagenesis, and consists of conserved Arg, Asn, Lys and Asp residues. The structural and binding studies taken together show that the cGMP binding GAF domains form a new class of cyclic nucleotide receptors distinct from the regulatory domains of cyclic nucleotide-regulated protein kinases and ion channels.
==About this Structure==
==About this Structure==
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1F5M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with BR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F5M OCA].
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1F5M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=BR:'>BR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5M OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Burden, L.M.]]
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[[Category: Burden, L M.]]
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[[Category: Ho, Y.S.]]
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[[Category: Ho, Y S.]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: BR]]
[[Category: BR]]
[[Category: cgmp binding]]
[[Category: cgmp binding]]
[[Category: gaf]]
[[Category: gaf]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:38:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:04 2008''

Revision as of 10:35, 21 February 2008


1f5m, resolution 1.9Å

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STRUCTURE OF THE GAF DOMAIN

Overview

GAF domains are ubiquitous motifs present in cyclic GMP (cGMP)-regulated cyclic nucleotide phosphodiesterases, certain adenylyl cyclases, the bacterial transcription factor FhlA, and hundreds of other signaling and sensory proteins from all three kingdoms of life. The crystal structure of the Saccharomyces cerevisiae YKG9 protein was determined at 1.9 A resolution. The structure revealed a fold that resembles the PAS domain, another ubiquitous signaling and sensory transducer. YKG9 does not bind cGMP, but the isolated first GAF domain of phosphodiesterase 5 binds with K:(d) = 650 nM. The cGMP binding site of the phosphodiesterase GAF domain was identified by homology modeling and site-directed mutagenesis, and consists of conserved Arg, Asn, Lys and Asp residues. The structural and binding studies taken together show that the cGMP binding GAF domains form a new class of cyclic nucleotide receptors distinct from the regulatory domains of cyclic nucleotide-regulated protein kinases and ion channels.

About this Structure

1F5M is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor., Ho YS, Burden LM, Hurley JH, EMBO J. 2000 Oct 16;19(20):5288-99. PMID:11032796

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