1CE2

STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION

Summary for 1CE2

• Entry DOI: 10.2210/pdb1ce2/pdb
• Descriptor: PROTEIN (LACTOFERRIN), FE (III) ION, CARBONATE ION, ... (4 entities in total)
• Functional Keywords: iron binding protein, lactoferrin, antibacterial, room temperature, metal transport
• Biological source: Bubalus bubalis (water buffalo)
• Total number of polymer chains: 1
• Total formula weight: 76077.95

Authors

Karthikeyan, S.,Paramasivam, M.,Yadav, S.,Srinivasan, A.,Singh, T.P. (deposition date: 1999-03-13, release date: 1999-03-19, Last modification date: 2024-10-30)

Primary citation

Karthikeyan, S.,Paramasivam, M.,Yadav, S.,Srinivasan, A.,Singh, T.P.
Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes.
Acta Crystallogr.,Sect.D, 55:1805-1813, 1999

PubMed Abstract: The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 A and Z = 4. The structure has been refined to an R factor of 0.187. The overall structure of the protein is similar to its structure determined at 277 K in a different crystal form. However, the lobe orientations in the two structures differ by 9.0 degrees, suggesting significant inter-lobe flexibility in this family of proteins. The inter-lobe interactions are predominantly hydrophobic and could act as a cushion for a change in orientation under the influence of external conditions. On the other hand, the domain arrangements are found to be similar in 277 and 303 K crystal structures, with orientations differing by 1.5 and 1.0 degrees in the N and C lobes, respectively. The results of these investigations suggest that the increase in temperature helps in the production of better quality crystals.

PubMed: 10531476
DOI: 10.1107/S0907444999010951

Experimental method

X-RAY DIFFRACTION (2.5 Å)