PDBsum entry 2ddd

Luminescent protein

PDB id: 2ddd

Contents

Protein chains

224 a.a. *

Metals

_NA ×2

_MG ×2

Waters ×600

* Residue conservation analysis

PDB id:

2ddd

Name:

Luminescent protein

Title:

Unique behavior of a histidine responsible for an engineered green-to- red photoconversion process

Structure:

Photoconvertible fluorescent protein. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Favia favus. Organism_taxid: 102203. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.55Å R-factor: 0.175 R-free: 0.190

Authors:

H.Shimizu,H.Tsutsui,N.Nukina,A.Miyawaki

Key ref:

H.Tsutsui et al. (2009). The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins. Chem Biol, 16, 1140-1147. PubMed id: 19942137

Date:

27-Jan-06 Release date: 07-Mar-06

Protein chains

Q53UG8  (Q53UG8_DIPFA) -  Photoconvertible fluorescent protein from Dipsastraea favus

Seq: 227 a.a.

Struc: 224 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Chem Biol 16:1140-1147 (2009)

PubMed id: 19942137

The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins.

H.Tsutsui, H.Shimizu, H.Mizuno, N.Nukina, T.Furuta, A.Miyawaki.

ABSTRACT

KikGR is a fluorescent protein engineered to display green-to-red photoconvertibility that is induced by irradiation with ultraviolet or violet light. Similar to Kaede and EosFP, two naturally occurring photoconvertible proteins, KikGR contains a His(62)-Tyr(63)-Gly(64) tripeptide sequence, which forms a green chromophore that can be photoconverted to a red one via formal beta-elimination and subsequent extension of a pi-conjugated system. Using a crystallizable variant of KikGR, we determined the structures of both the green and red state at 1.55 A resolution. The double bond between His(62)-C(alpha) and His(62)-C(beta) in the red chromophore is in a cis configuration, indicating that rotation along the His(62) C(alpha)-C(beta) bond occurs following cleavage of the His(62) N(alpha)-C(alpha) bond. This structural rearrangement provides evidence that the beta-elimination reaction governing the green-to-red photoconversion of KikGR follows an E1 (elimination, unimolecular) mechanism.