PDBsum entry 7a8c

Fluorescent protein

PDB id: 7a8c

Contents

Protein chain

226 a.a.

Ligands

PGE

Waters ×169

PDB id:

7a8c

Name:

Fluorescent protein

Title:

Rsgreen0.7-k206a-f145s in the green-off state

Structure:

Green fluorescent protein. Chain: a. Engineered: yes

Source:

Aequorea victoria. Jellyfish. Organism_taxid: 6100. Gene: gfp. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: jm109

Resolution:

2.13Å R-factor: 0.204 R-free: 0.253

Authors:

E.De Zitter,P.Dedecker,L.Van Meervelt

Key ref:

E.De Zitter et al. (2021). Structure-Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System*. Angew Chem Int Ed Engl, 60, 10073-10081. PubMed id: 33543524 DOI: 10.1002/anie.202015201

Date:

30-Aug-20 Release date: 17-Feb-21

Protein chain

A0A059PIQ0  (A0A059PIQ0_AEQVI) -  Green fluorescent protein (Fragment) from Aequorea victoria

Seq: 251 a.a.

Struc: 226 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1002/anie.202015201

Angew Chem Int Ed Engl 60:10073-10081 (2021)

PubMed id: 33543524

Structure-Function Dataset Reveals Environment Effects within a Fluorescent Protein Model System*.

E.De Zitter, S.Hugelier, S.Duwé, W.Vandenberg, A.G.Tebo, L.Van Meervelt, P.Dedecker.

ABSTRACT

Anisotropic environments can drastically alter the spectroscopy and photochemistry of molecules, leading to complex structure-function relationships. We examined this using fluorescent proteins as easy-to-modify model systems. Starting from a single scaffold, we have developed a range of 27 photochromic fluorescent proteins that cover a broad range of spectroscopic properties, including the determination of 43 crystal structures. Correlation and principal component analysis confirmed the complex relationship between structure and spectroscopy, but also allowed us to identify consistent trends and to relate these to the spatial organization. We find that changes in spectroscopic properties can come about through multiple underlying mechanisms, of which polarity, hydrogen bonding and presence of water molecules are key modulators. We anticipate that our findings and rich structure/spectroscopy dataset can open opportunities for the development and evaluation of new and existing protein engineering methods.