Structure of buffalo lactoferrin at 3.3 angstrom resolution at 277 K

Citation
S. Karthikeyan et al., Structure of buffalo lactoferrin at 3.3 angstrom resolution at 277 K, ACT CRYST D, 56, 2000, pp. 684-689
Citations number
29
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
0907-4449 → ACNP
Volume
56
Year of publication
2000
Part
6
Pages
684 - 689
Database
ISI
SICI code
0907-4449(200006)56:<684:SOBLA3>2.0.ZU;2-#
Abstract
The three-dimensional structure of diferric buffalo lactoferrin has been de termined at 3.3 Angstrom resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-PLOR). The final model com prises 5316 protein atoms for all 689 residues, two Fe3+ and two CO32- ions . The final R factor was 21.8% for 11 711 reflections in the resolution ran ge 17.0-3.3 Angstrom. The folding of buffalo lactoferrin is essentially sim ilar to that of the other members of the transferrin family. The significan t differences are found in the dimensions of the binding cleft and the inte rlobe orientation. The interlobe interactions are predominantly hydrophobic in nature, thus facilitating the sliding of two lobes owing to external fo rces. The interdomain interactions are comparable in the N and C lobes.