2c9j

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{{Seed}}
 
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[[Image:2c9j.png|left|200px]]
 
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==Structure of the fluorescent protein cmFP512 at 1.35A from Cerianthus membranaceus==
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The line below this paragraph, containing "STRUCTURE_2c9j", creates the "Structure Box" on the page.
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<StructureSection load='2c9j' size='340' side='right'caption='[[2c9j]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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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'>[[2c9j]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cerianthus_membranaceus Cerianthus membranaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9J FirstGlance]. <br>
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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]] 1.35&#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=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene></td></tr>
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{{STRUCTURE_2c9j| PDB=2c9j | 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=2c9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9j OCA], [https://pdbe.org/2c9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9j RCSB], [https://www.ebi.ac.uk/pdbsum/2c9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q5ZQQ5_CERMM Q5ZQQ5_CERMM]
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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/c9/2c9j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2c9j 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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Autofluorescent proteins of the GFP family all share the same three-dimensional beta-can fold; yet they exhibit widely different optical properties, arising either from chemical modification of the chromophore itself or from specific interactions of the chromophore with the surrounding protein moiety. Here we present a structural and spectroscopic characterization of the green fluorescent protein cmFP512 from Cerianthus membranaceus, a nonbioluminescent, azooxanthellate cnidarian, which has only approximately 22% sequence identity with Aequorea victoria GFP. The X-ray structure, obtained by molecular replacement at a resolution of 1. 35 A, shows the chromophore, formed from the tripeptide Gln-Tyr-Gly, in a hydrogen-bonded cage in the center of an 11-stranded beta-barrel, tightly restrained by adjacent residues and structural water molecules. It exists in a neutral (A) and an anionic (B) species, with absorption/emission maxima at 392/460 (pH 5) and 503/512 nm (pH 7). Their fractional populations and peak positions depend sensitively on pH, reflecting protonation of groups adjacent to the chromophore. The pH dependence of the spectra is explained by a protonation mechanism involving a hydrogen-bonded cluster of charged/polar groups. Cryospectroscopy at 12 K was also performed to analyze the vibronic coupling of the electronic transitions.
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===STRUCTURE OF THE FLUORESCENT PROTEIN CMFP512 AT 1.35A FROM CERIANTHUS MEMBRANACEUS===
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Exploring chromophore--protein interactions in fluorescent protein cmFP512 from Cerianthus membranaceus: X-ray structure analysis and optical spectroscopy.,Nienhaus K, Renzi F, Vallone B, Wiedenmann J, Nienhaus GU Biochemistry. 2006 Oct 31;45(43):12942-53. PMID:17059211<ref>PMID:17059211</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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<div class="pdbe-citations 2c9j" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17059211}}, adds the Publication Abstract to the page
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*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17059211 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17059211}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2C9J is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Cerianthus_membranaceus Cerianthus membranaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9J OCA].
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==Reference==
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<ref group="xtra">PMID:17059211</ref><references group="xtra"/>
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[[Category: Cerianthus membranaceus]]
[[Category: Cerianthus membranaceus]]
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[[Category: Nienhaus, G U.]]
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[[Category: Large Structures]]
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[[Category: Nienhaus, K.]]
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[[Category: Nienhaus GU]]
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[[Category: Renzi, F.]]
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[[Category: Nienhaus K]]
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[[Category: Vallone, B.]]
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[[Category: Renzi F]]
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[[Category: Wiedenmann, J.]]
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[[Category: Vallone B]]
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[[Category: Beta-barrel]]
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[[Category: Wiedenmann J]]
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[[Category: Bioluminescence]]
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[[Category: Fluorescent protein]]
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[[Category: Luminescence]]
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[[Category: Luminescent protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:47:30 2009''
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Current revision

Structure of the fluorescent protein cmFP512 at 1.35A from Cerianthus membranaceus

PDB ID 2c9j

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