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[[Image:1yhh.gif|left|200px]]


{{Structure
==Uncyclized precursor structure of S65A Y66S G67A GFP variant==
|PDB= 1yhh |SIZE=350|CAPTION= <scene name='initialview01'>1yhh</scene>, resolution 1.500&Aring;
<StructureSection load='1yhh' size='340' side='right'caption='[[1yhh]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1yhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YHH FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yhh OCA], [https://pdbe.org/1yhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yhh RCSB], [https://www.ebi.ac.uk/pdbsum/1yhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yhh ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
== 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/yh/1yhh_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=1yhh ConSurf].
<div style="clear:both"></div>


'''Uncyclized precursor structure of S65A Y66S G67A GFP variant'''
==See Also==
 
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The Aequorea victoria green fluorescent protein (GFP) undergoes a remarkable post-translational modification to create a chromophore out of its component amino acids S65, Y66, and G67. Here, we describe mutational experiments in GFP designed to convert this chromophore into a 4-methylidene-imidazole-5-one (MIO) moiety similar to the post-translational active-site electrophile of histidine ammonia lyase (HAL). Crystallographic structures of GFP variant S65A Y66S (GFPhal) and of four additional related site-directed mutants reveal an aromatic MIO moiety and mechanistic details of GFP chromophore formation and MIO biosynthesis. Specifically, the GFP scaffold promotes backbone cyclization by (1) favoring nucleophilic attack by close proximity alignment of the G67 amide lone pair with the pi orbital of the residue 65 carbonyl and (2) removing enthalpic barriers by eliminating inhibitory main-chain hydrogen bonds in the precursor state. GFP R96 appears to induce structural rearrangements important in aligning the molecular orbitals for ring cyclization, favor G67 nitrogen deprotonation through electrostatic interactions with the Y66 carbonyl, and stabilize the reduced enolate intermediate. Our structures and analysis also highlight negative design features of the wild-type GFP architecture, which favor chromophore formation by destabilizing alternative conformations of the chromophore tripeptide. By providing a molecular basis for understanding and controlling the driving force and protein chemistry of chromophore creation, this research has implications for expansion of the genetic code through engineering of modified amino acids.
 
==About this Structure==
1YHH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YHH OCA].
 
==Reference==
Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry., Barondeau DP, Kassmann CJ, Tainer JA, Getzoff ED, Biochemistry. 2005 Feb 15;44(6):1960-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697221 15697221]
[[Category: Aequorea victoria]]
[[Category: Aequorea victoria]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barondeau, D P.]]
[[Category: Barondeau DP]]
[[Category: Getzoff, E D.]]
[[Category: Getzoff ED]]
[[Category: Kassmann, C J.]]
[[Category: Kassmann CJ]]
[[Category: Tainer, J A.]]
[[Category: Tainer JA]]
[[Category: chromophore]]
[[Category: coil-to-helix]]
[[Category: uncyclized]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:22:53 2008''

Latest revision as of 11:57, 14 February 2024

Uncyclized precursor structure of S65A Y66S G67A GFP variantUncyclized precursor structure of S65A Y66S G67A GFP variant

Structural highlights

1yhh is a 1 chain structure with sequence from Aequorea victoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.

Evolutionary Conservation

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

See Also

1yhh, resolution 1.50Å

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