1f5m
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1f5m.jpg|left|200px]] | + | [[Image:1f5m.jpg|left|200px]] |
- | + | ||
- | '''STRUCTURE OF THE GAF DOMAIN''' | + | {{Structure |
+ | |PDB= 1f5m |SIZE=350|CAPTION= <scene name='initialview01'>1f5m</scene>, resolution 1.9Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF THE GAF DOMAIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1F5M is a [ | + | 1F5M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F5M OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11032796 11032796] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 20: | Line 29: | ||
[[Category: gaf]] | [[Category: gaf]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:45 2008'' |
Revision as of 09:04, 20 March 2008
| |||||||
, resolution 1.9Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
Page seeded by OCA on Thu Mar 20 11:04:45 2008