7Q1L

Glycosilated Human Serum Apo-tranferrin

Summary for 7Q1L

• Entry DOI: 10.2210/pdb7q1l/pdb
• Descriptor: Serotransferrin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (7 entities in total)
• Functional Keywords: serotransferrin, iron-free (apo), metal transport
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 151808.35

Authors

Gavira, J.A.,Moreno, A.,Campos-Escamilla, C.,Gonzalez-Ramirez, L.A.,Siliqi, D. (deposition date: 2021-10-20, release date: 2022-03-16, Last modification date: 2024-10-16)

Primary citation

Campos-Escamilla, C.,Siliqi, D.,Gonzalez-Ramirez, L.A.,Lopez-Sanchez, C.,Gavira, J.A.,Moreno, A.
X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: Human serum transferrin (Tf) is a bilobed glycoprotein whose function is to transport iron through receptor-mediated endocytosis. The mechanism for iron release is pH-dependent and involves conformational changes in the protein, thus making it an attractive system for possible biomedical applications. In this contribution, two powerful X-ray techniques, namely Macromolecular X-ray Crystallography (MX) and Small Angle X-ray Scattering (SAXS), were used to study the conformational changes of iron-free (apo) and iron-loaded (holo) transferrin in crystal and solution states, respectively, at three different pH values of physiological relevance. A crystallographic model of glycosylated apo-Tf was obtained at 3.0 Å resolution, which did not resolve further despite many efforts to improve crystal quality. In the solution, apo-Tf remained mostly globular in all the pH conditions tested; however, the co-existence of closed, partially open, and open conformations was observed for holo-Tf, which showed a more elongated and flexible shape overall.

PubMed: 34948188
DOI: 10.3390/ijms222413392

Experimental method

X-RAY DIFFRACTION (3 Å)