Ontology highlight
ABSTRACT:
SUBMITTER: Thompson GS
PROVIDER: S-EPMC2144627 | biostudies-other | 2000 May
REPOSITORIES: biostudies-other
Thompson G S GS Leung Y C YC Ferguson S J SJ Radford S E SE Redfield C C
Protein science : a publication of the Protein Society 20000501 5
The solution structure and backbone dynamics of Cu(I) pseudoazurin, a 123 amino acid electron transfer protein from Paracoccus pantotrophus, have been determined using NMR methods. The structure was calculated to high precision, with a backbone RMS deviation for secondary structure elements of 0.35+/-0.06 A, using 1,498 distance and 55 torsion angle constraints. The protein has a double-wound Greek-key fold with two alpha-helices toward its C-terminus, similar to that of its oxidized counterpart ...[more]