1MR8

MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN

Summary for 1MR8

• Entry DOI: 10.2210/pdb1mr8/pdb
• Descriptor: MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8, CALCIUM ION (3 entities in total)
• Functional Keywords: calcium-binding protein, mad, migration inhibitory factor_ related protein 8, s100 protein, metal transport
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P05109
• Total number of polymer chains: 2
• Total formula weight: 21867.37

Authors

Ishikawa, K.,Nakagawa, A.,Tanaka, I.,Nishihira, J. (deposition date: 1999-04-13, release date: 2000-05-17, Last modification date: 2023-12-27)

Primary citation

Ishikawa, K.,Nakagawa, A.,Tanaka, I.,Suzuki, M.,Nishihira, J.
The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution.
Acta Crystallogr.,Sect.D, 56:559-566, 2000

PubMed Abstract: The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.

PubMed: 10771424
DOI: 10.1107/S0907444900002833

Experimental method

X-RAY DIFFRACTION (1.9 Å)