1PP3

Structure of thaumatin in a hexagonal space group

Summary for 1PP3

• Entry DOI: 10.2210/pdb1pp3/pdb
• Descriptor: Thaumatin I (2 entities in total)
• Functional Keywords: plant protein
• Biological source: Thaumatococcus daniellii (miracle fruit)
• Cellular location: Cytoplasmic vesicle: P02883
• Total number of polymer chains: 2
• Total formula weight: 44454.12

Authors

Charron, C.,Giege, R.,Lorber, B. (deposition date: 2003-06-16, release date: 2004-08-10, Last modification date: 2024-10-30)

Primary citation

Charron, C.,Giege, R.,Lorber, B.
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.
Acta Crystallogr.,Sect.D, 60:83-89, 2004

PubMed Abstract: The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.

PubMed: 14684896

Experimental method

X-RAY DIFFRACTION (1.6 Å)