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==STRUCTURE OF THE FLUORESCENT PROTEIN CMFP512 AT 1.35A FROM CERIANTHUS MEMBRANACEUS==
 
<StructureSection load='2c9j' size='340' side='right' caption='[[2c9j]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
==Structure of the fluorescent protein cmFP512 at 1.35A from Cerianthus membranaceus==
<StructureSection load='2c9j' size='340' side='right'caption='[[2c9j]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c9j]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Cermm Cermm]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9J FirstGlance]. <br>
<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>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b9c|1b9c]], [[1bfp|1bfp]], [[1c4f|1c4f]], [[1ema|1ema]], [[1emb|1emb]], [[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emg|1emg]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[1f09|1f09]], [[1f0b|1f0b]], [[1g7k|1g7k]], [[1gfl|1gfl]], [[1ggx|1ggx]], [[1h6r|1h6r]], [[1hcj|1hcj]], [[1huy|1huy]], [[1jby|1jby]], [[1jbz|1jbz]], [[1jc0|1jc0]], [[1jc1|1jc1]], [[1kp5|1kp5]], [[1kyp|1kyp]], [[1kyr|1kyr]], [[1kys|1kys]], [[1myw|1myw]], [[1oxd|1oxd]], [[1oxe|1oxe]], [[1oxf|1oxf]], [[1q4a|1q4a]], [[1q4b|1q4b]], [[1q4c|1q4c]], [[1q4d|1q4d]], [[1q4e|1q4e]], [[1q73|1q73]], [[1qxt|1qxt]], [[1qy3|1qy3]], [[1qyf|1qyf]], [[1rm9|1rm9]], [[1rmm|1rmm]], [[1rmo|1rmo]], [[1rmp|1rmp]], [[1rrx|1rrx]], [[1s6z|1s6z]], [[1w7s|1w7s]], [[1w7t|1w7t]], [[1w7u|1w7u]], [[1xa9|1xa9]], [[1xae|1xae]], [[1xss|1xss]], [[1yjf|1yjf]], [[1z1p|1z1p]], [[1z1q|1z1q]], [[1zgo|1zgo]], [[1zgp|1zgp]], [[1zgq|1zgq]], [[1zux|1zux]], [[2a46|2a46]], [[2a50|2a50]], [[2a52|2a52]], [[2a53|2a53]], [[2a54|2a54]], [[2a56|2a56]], [[2b3p|2b3p]], [[2b3q|2b3q]], [[2btj|2btj]], [[2emd|2emd]], [[2emn|2emn]], [[2emo|2emo]], [[2c9i|2c9i]]</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9j OCA], [http://pdbe.org/2c9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9j RCSB], [http://www.ebi.ac.uk/pdbsum/2c9j PDBsum]</span></td></tr>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5ZQQ5_CERMM Q5ZQQ5_CERMM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9j_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9j_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[Green Fluorescent Protein|Green Fluorescent Protein]]
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cermm]]
[[Category: Cerianthus membranaceus]]
[[Category: Nienhaus, G U]]
[[Category: Large Structures]]
[[Category: Nienhaus, K]]
[[Category: Nienhaus GU]]
[[Category: Renzi, F]]
[[Category: Nienhaus K]]
[[Category: Vallone, B]]
[[Category: Renzi F]]
[[Category: Wiedenmann, J]]
[[Category: Vallone B]]
[[Category: Beta-barrel]]
[[Category: Wiedenmann J]]
[[Category: Bioluminescence]]
[[Category: Fluorescent protein]]
[[Category: Luminescence]]
[[Category: Luminescent protein]]

Latest revision as of 11:19, 15 November 2023

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

Structural highlights

2c9j is a 8 chain structure with sequence from Cerianthus membranaceus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5ZQQ5_CERMM

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Nienhaus K, Renzi F, Vallone B, Wiedenmann J, Nienhaus GU. Exploring chromophore--protein interactions in fluorescent protein cmFP512 from Cerianthus membranaceus: X-ray structure analysis and optical spectroscopy. Biochemistry. 2006 Oct 31;45(43):12942-53. PMID:17059211 doi:10.1021/bi060885c

2c9j, resolution 1.35Å

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OCA