PDBsum entry 1kp5

Luminescent protein

PDB id: 1kp5

Contents

Protein chains

243 a.a. *

Ligands

SO4 ×8

Waters ×94

* Residue conservation analysis

PDB id:

1kp5

Name:

Luminescent protein

Title:

Cyclic green fluorescent protein

Structure:

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

Source:

Aequorea victoria. Organism_taxid: 6100. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.60Å R-factor: 0.208 R-free: 0.256

Authors:

A.Hofmann,H.Iwai,A.Plueckthun,A.Wlodawer

Key ref:

A.Hofmann et al. (2002). Structure of cyclized green fluorescent protein. Acta Crystallogr D Biol Crystallogr, 58, 1400-1406. PubMed id: 12198295 DOI: 10.1107/S0907444902010454

Date:

28-Dec-01 Release date: 28-Aug-02

Protein chains

P42212  (GFP_AEQVI) -  Green fluorescent protein from Aequorea victoria

Seq: 238 a.a.

Struc: 243 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1107/S0907444902010454

Acta Crystallogr D Biol Crystallogr 58:1400-1406 (2002)

PubMed id: 12198295

Structure of cyclized green fluorescent protein.

A.Hofmann, H.Iwai, S.Hess, A.Plückthun, A.Wlodawer.

ABSTRACT

Crystals of cyclic green fluorescent protein (cGFP) engineered by the previously reported split intein technology [Iwai et al. (2001), J. Biol. Chem. 276, 16548-16554] were obtained and the structure was solved using molecular replacement. Although the core of the protein can unambiguously be fitted from the first to the last residue of the genuine sequence, the electron density in the region of the linker peptide is rather poor owing to the high water content of the crystals. Therefore, it is concluded that this part of the protein is highly disordered in the present structure and is very flexible. This is supported by the absence of crystal contacts in the linker-peptide region and the fact that the core of the protein exhibits a very similar conformation to that known from other GFP structures, thereby not implicating any constraints arising from the presence of the artificial linker. Nevertheless, the density is consistent with the loop being intact, as confirmed by mass spectroscopy of dissolved crystals. The present structure contains an antiparallel cGFP dimer where the dimer interface is clearly different from other crystal structures featuring two GFP molecules. This adds further support to the fact that the cylinder surface of GFP is rather versatile and can employ various polar and non-polar patches in protein-protein interactions.

Selected figure(s)

Figure 2.
Figure 2 The cGFP dimer. Molecule #1 is colored in blue and molecule #2 in dark red. For each molecule the artificial linker is shown in red and the chromophore as well as the preceding and the following residues are drawn explicitly (green and yellow). The figure was created with MOLSCRIPT/BOBSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]; Esnouf, 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.]) and rendered with POVRay (Persistence of Vision Development Team, 1999[Persistence of Vision Development Team (1999). POVRay - The Persistence of Vision Raytracer, http://www.povray.org .]).

Figure 4.
Figure 4 The dimer interface. The explosion figure of the dimer interface shows molecule #1 on the left and molecule #2 on the right. The figure was created with GRASP (Nicholls, 1992[Nicholls, A. (1992). GRASP: Graphical Representation and Analysis of Surface Properties. Columbia University, New York, USA.]).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1400-1406) copyright 2002.

Figures were selected by an automated process.