1f5m

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{{Seed}}
 
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[[Image:1f5m.png|left|200px]]
 
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==STRUCTURE OF THE GAF DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1f5m", creates the "Structure Box" on the page.
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<StructureSection load='1f5m' size='340' side='right'caption='[[1f5m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1f5m]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F5M FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
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{{STRUCTURE_1f5m| PDB=1f5m | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5m OCA], [https://pdbe.org/1f5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f5m RCSB], [https://www.ebi.ac.uk/pdbsum/1f5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f5m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FRMSR_YEAST FRMSR_YEAST] Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.<ref>PMID:19049972</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/1f5m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f5m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===STRUCTURE OF THE GAF DOMAIN===
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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<ref>PMID:11032796</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11032796}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1f5m" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11032796 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11032796}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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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].
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==Reference==
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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]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Burden LM]]
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[[Category: Burden, L M.]]
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[[Category: Ho YS]]
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[[Category: Ho, Y S.]]
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[[Category: Hurley JH]]
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[[Category: Hurley, J H.]]
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[[Category: Cgmp binding]]
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[[Category: Gaf]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:44:08 2008''
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Current revision

STRUCTURE OF THE GAF DOMAIN

PDB ID 1f5m

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