2zo7: Difference between revisions
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< | ==Crystal Structure of a Kusabira-Cyan Mutant (KCY-R1), a Cyan/Green-Emitting GFP-Like Protein== | ||
<StructureSection load='2zo7' size='340' side='right'caption='[[2zo7]], [[Resolution|resolution]] 1.58Å' scene=''> | |||
You may | == Structural highlights == | ||
or the | <table><tr><td colspan='2'>[[2zo7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithophyllon_concinna Lithophyllon concinna]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2eji 2eji]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZO7 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></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=2zo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zo7 OCA], [https://pdbe.org/2zo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zo7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zo7 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/2zo7_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/main_output.php?pdb_ID=2zo7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Green fluorescent protein (GFP) based techniques are well established in molecular biology; however, the detailed mechanism for the fine-tuning of fluorescent colors remains unclear. Here, we report the cloning and crystal structure of a new cyan-emitting GFP-like protein, KCy. We also developed a mutant protein with a high folding efficiency (KCy-G4219: lambda(abs) = 453 nm; lambda(em) = 486 nm). X-ray diffraction analysis revealed that the KCy chromophore is formed from an internal Ser62-Tyr63-Gly64 tripeptide. The serine residue at the first position of the chromophore-forming tripeptide has a short polar chain (-OH) that forms a noncovalent interaction with the His38 imidazole at a distance of 2.96 A. Substitution of His38 in KCy-G4219 with Gln (KCy-R1) or Leu residues resulted in a slight but significant red shift of the emission peak maximum from 486 to 492 or 496 nm, respectively. The crystal structure of KCy-R1 determined at a resolution of 1.58 A showed that the noncovalent interaction between Ser62-OH and the substituted Gln38 occurred over a longer distance (3.07 A) than that observed in the wild-type KCy. Such an interaction is absent in the Leu mutant, suggesting that this interaction is one of the key factors responsible for fine-tuning the emission peak maxima, which are affected by chromophore polarization. Moreover, the structural comparison suggests that an additional water molecule buried in the space between the Ala158 residue and the chromophore phenolate is also responsible for the chromophore polarization. | |||
Crystal structure of a new cyan fluorescent protein and its hue-shifted variants.,Kikuchi A, Fukumura E, Karasawa S, Shiro Y, Miyawaki A Biochemistry. 2009 Jun 16;48(23):5276-83. PMID:19402703<ref>PMID:19402703</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2zo7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | [[Category: Lithophyllon concinna]] | ||
[[Category: Fukumura E]] | |||
== | [[Category: Karasawa S]] | ||
< | [[Category: Kikuchi A]] | ||
[[Category: | [[Category: Miyawaki A]] | ||
[[Category: Fukumura | [[Category: Shiro Y]] | ||
[[Category: Karasawa | |||
[[Category: Kikuchi | |||
[[Category: Miyawaki | |||
[[Category: Shiro | |||
Latest revision as of 16:46, 1 November 2023
Crystal Structure of a Kusabira-Cyan Mutant (KCY-R1), a Cyan/Green-Emitting GFP-Like ProteinCrystal Structure of a Kusabira-Cyan Mutant (KCY-R1), a Cyan/Green-Emitting GFP-Like Protein
Structural highlights
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 PubMedGreen fluorescent protein (GFP) based techniques are well established in molecular biology; however, the detailed mechanism for the fine-tuning of fluorescent colors remains unclear. Here, we report the cloning and crystal structure of a new cyan-emitting GFP-like protein, KCy. We also developed a mutant protein with a high folding efficiency (KCy-G4219: lambda(abs) = 453 nm; lambda(em) = 486 nm). X-ray diffraction analysis revealed that the KCy chromophore is formed from an internal Ser62-Tyr63-Gly64 tripeptide. The serine residue at the first position of the chromophore-forming tripeptide has a short polar chain (-OH) that forms a noncovalent interaction with the His38 imidazole at a distance of 2.96 A. Substitution of His38 in KCy-G4219 with Gln (KCy-R1) or Leu residues resulted in a slight but significant red shift of the emission peak maximum from 486 to 492 or 496 nm, respectively. The crystal structure of KCy-R1 determined at a resolution of 1.58 A showed that the noncovalent interaction between Ser62-OH and the substituted Gln38 occurred over a longer distance (3.07 A) than that observed in the wild-type KCy. Such an interaction is absent in the Leu mutant, suggesting that this interaction is one of the key factors responsible for fine-tuning the emission peak maxima, which are affected by chromophore polarization. Moreover, the structural comparison suggests that an additional water molecule buried in the space between the Ala158 residue and the chromophore phenolate is also responsible for the chromophore polarization. Crystal structure of a new cyan fluorescent protein and its hue-shifted variants.,Kikuchi A, Fukumura E, Karasawa S, Shiro Y, Miyawaki A Biochemistry. 2009 Jun 16;48(23):5276-83. PMID:19402703[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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