1EMA

GREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA

PDB DOI: https://doi.org/10.2210/pdb1EMA/pdb

Classification: FLUORESCENT PROTEIN
Organism(s): Aequorea victoria
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 1996-08-01 Released: 1996-11-08
Deposition Author(s): Ormo, M., Remington, S.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal structure of the Aequorea victoria green fluorescent protein.

Ormo, M., Cubitt, A.B., Kallio, K., Gross, L.A., Tsien, R.Y., Remington, S.J.

(1996) Science 273: 1392-1395

PubMed: 8703075 Search on PubMed
DOI: https://doi.org/10.1126/science.273.5280.1392
Primary Citation of Related Structures:
1EMA

PubMed Abstract:
The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products. The chromophore, resulting from the spontaneous cyclization and oxidation of the sequence -Ser65 (or Thr65)-Tyr66-Gly67-, requires the native protein fold for both formation and fluorescence emission. The structure of Thr65 GFP has been determined at 1.9 angstrom resolution. The protein fold consists of an 11-stranded beta barrel with a coaxial helix, with the chromophore forming from the central helix. Directed mutagenesis of one residue adjacent to the chromophore, Thr203, to Tyr or His results in significantly red-shifted excitation and emission maxima.

Organizational Affiliation

Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, OR 97403-1226, USA.

Macromolecule Content

Total Structure Weight: 27.23 kDa
Atom Count: 1,866
Modelled Residue Count: 226
Deposited Residue Count: 236
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
GREEN FLUORESCENT PROTEIN	A	236	Aequorea victoria	Mutation(s): 1
UniProt
Find proteins for P42212 (Aequorea victoria) Explore P42212 Go to UniProtKB: P42212
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P42212
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 2 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
CRO Query on CRO	A	L-PEPTIDE LINKING	C₁₅ H₁₇ N₃ O₅		THR, TYR, GLY
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 51.77	α = 90
b = 62.85	β = 90
c = 70.67	γ = 90

Software Package:

Software Name	Purpose
CCP4	model building
PROTEIN	model building
TNT	refinement
HKL	data reduction
HKL	data scaling
CCP4	phasing
PROTEIN	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1996-11-08

Deposition Author(s):

Remington, S.J.

Revision History (Full details and data files)

Version 1.0: 1996-11-08
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.