1JGY

Photosynthetic Reaction Center Mutant With Tyr M 76 Replaced With Phe

Summary for 1JGY

• Entry DOI: 10.2210/pdb1jgy/pdb
• Related: 1JGW 1JGX 1JGZ 1JH0
• Descriptor: Photosynthetic Reaction Center L Subunit, Photosynthetic Reaction Center M Subunit, Photosynthetic Reaction Center H Subunit, ... (10 entities in total)
• Functional Keywords: alpha helix, photosynthesis
• Biological source: Rhodobacter sphaeroides; More
• Cellular location: Cellular chromatophore membrane; Multi-pass membrane protein: P02954 P02953; Cellular chromatophore membrane; Single-pass membrane protein: P11846
• Total number of polymer chains: 3
• Total formula weight: 102171.85

Authors

Camara-Artigas, A.,Magee, C.L.,Williams, J.C.,Allen, J.P. (deposition date: 2001-06-27, release date: 2001-09-05, Last modification date: 2023-08-16)

Primary citation

Camara-Artigas, A.,Magee, C.L.,Williams, J.C.,Allen, J.P.
Individual interactions influence the crystalline order for membrane proteins.
Acta Crystallogr.,Sect.D, 57:1281-1286, 2001

PubMed Abstract: The role of contact interactions in the crystallization of membrane proteins was assessed by mutation of amino-acid residues on the surface of the reaction center from Rhodobacter sphaeroides. Five single-site mutants were constructed, with changes in contact regions found in the trigonal and tetragonal forms but not the orthorhombic form. Crystallization trials for the tetragonal form yielded either no crystals or crystals with an altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the tetragonal crystals. Changes in the structures determined by X-ray diffraction of trigonal crystals for each mutant were related to the quality of the diffraction. Significant differences in the resolution limit of the crystals were associated with the loss of specific interactions between neighboring proteins. The results suggest that the contact regions are crucial for obtaining highly ordered crystals of membrane proteins.

PubMed: 11526320
DOI: 10.1107/S090744490101109X

Experimental method

X-RAY DIFFRACTION (2.7 Å)