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2c9j

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Revision as of 08:37, 23 May 2018

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

Structural highlights

2c9j is a 8 chain structure with sequence from Cermm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1b9c, 1bfp, 1c4f, 1ema, 1emb, 1emc, 1eme, 1emf, 1emg, 1emk, 1eml, 1emm, 1f09, 1f0b, 1g7k, 1gfl, 1ggx, 1h6r, 1hcj, 1huy, 1jby, 1jbz, 1jc0, 1jc1, 1kp5, 1kyp, 1kyr, 1kys, 1myw, 1oxd, 1oxe, 1oxf, 1q4a, 1q4b, 1q4c, 1q4d, 1q4e, 1q73, 1qxt, 1qy3, 1qyf, 1rm9, 1rmm, 1rmo, 1rmp, 1rrx, 1s6z, 1w7s, 1w7t, 1w7u, 1xa9, 1xae, 1xss, 1yjf, 1z1p, 1z1q, 1zgo, 1zgp, 1zgq, 1zux, 2a46, 2a50, 2a52, 2a53, 2a54, 2a56, 2b3p, 2b3q, 2btj, 2emd, 2emn, 2emo, 2c9i
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

↑ 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

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c9j"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF THE FLUORESCENT PROTEIN CMFP512 AT 1.35A FROM CERIANTHUS MEMBRANACEUS==
+==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 ==
@@ Line 5: / Line 6: @@
 </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>
 <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='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'>[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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9j ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <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>
     <text>to colour the structure by Evolutionary Conservation</text>
   </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="background-color:#fffaf0;">

2c9j

From Proteopedia

Revision as of 08:37, 23 May 2018

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

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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