PDBsum entry: 1gsv

Photosynthesis

PDB id: 1gsv

Contents

Protein chain

122 a.a. *

Ligands

HC4

Waters ×75

* Residue conservation analysis

PDB id:

1gsv

Name:

Photosynthesis

Title:

Crystal structure of the p65 crystal form of photoactive yellow protein g47s mutant

Structure:

Photoactive yellow protein. Chain: a. Synonym: pyp. Engineered: yes. Mutation: yes

Source:

Ectothiorhodospira halophila. Organism_taxid: 1053. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.75Å R-factor: 0.191 R-free: 0.246

Authors:

D.M.F.Van Aalten,W.Crielaard,K.J.Hellingwerf,L.Joshua-Tor

Key ref:

D.M.van Aalten et al. (2002). Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants. J Biol Chem, 277, 6463-6468. PubMed id: 11714713 DOI: 10.1074/jbc.M109313200

Date:

08-Jan-02 Release date: 14-Feb-02

Protein chain

P16113  (PYP_HALHA) -  Photoactive yellow protein

Seq: 125 a.a.

Struc: 122 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: response to stimulus (5 terms)
• Biochemical function: signal transducer activity (3 terms)

DOI no: 10.1074/jbc.M109313200

J Biol Chem 277:6463-6468 (2002)

PubMed id: 11714713

Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants.

D.M.van Aalten, A.Haker, J.Hendriks, K.J.Hellingwerf, L.Joshua-Tor, W.Crielaard.

ABSTRACT

Crystallographic and spectroscopic analyses of three hinge-bending mutants of the photoactive yellow protein are described. Previous studies have identified Gly(47) and Gly(51) as possible hinge points in the structure of the protein, allowing backbone segments around the chromophore to undergo large concerted motions. We have designed, crystallized, and solved the structures of three mutants: G47S, G51S, and G47S/G51S. The protein dynamics of these mutants are significantly affected. Transitions in the photocycle, measured with laser induced transient absorption spectroscopy, show rates up to 6-fold different from the wild type protein and show an additive effect in the double mutant. Compared with the native structure, no significant conformational differences were observed in the structures of the mutant proteins. We conclude that the structural and dynamic integrity of the region around these mutations is of crucial importance to the photocycle and suggest that the hinge-bending properties of Gly(51) may also play a role in PAS domain proteins where it is one of the few conserved residues.

Selected figure(s)

Figure 3.
Fig. 3. Conformational changes for residues 47-61. The backbone of WTPYP is drawn in a gray ribbon representation with the chromophore drawn in a magenta sticks representation. For PYP47 (green), PYP51 (red), and PYP47+51 (blue), a C -trace and side chain atoms are shown for residues 47-61, which are further identified with labels.

Figure 4.
Fig. 4. Ramachandran plots of residues 47-61 in WTPYP and mutant structures.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 6463-6468) copyright 2002.

Figures were selected by an automated process.