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207 a.a.
Key reference
DOI no: 10.1107/S0907444903022613 Acta Crystallogr D Biol Crystallogr 60:83-89 (2004) PubMed id: 14684896
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices. C.Charron, R.Giegé, B.Lorber. 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.
Literature references that cite this PDB file's key reference
PubMed id Reference
15703077 R.Kant (2005).
Sweet proteins--potential replacement for artificial low calorie sweeteners.Nutr J, 4, 5. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.
