2ZRS

Crystal structure of Ca2+-bound form of des3-23ALG-2

Summary for 2ZRS

• Entry DOI: 10.2210/pdb2zrs/pdb
• Related: 2ZN9 2ZND 2ZNE 2ZRT
• Descriptor: Programmed cell death protein 6, CALCIUM ION (2 entities in total)
• Functional Keywords: penta-ef-hand protein, calcium-binding protein, apoptosis, calcium, endoplasmic reticulum, membrane, nucleus, polymorphism
• Biological source: Homo sapiens (Human)
• Cellular location: Endoplasmic reticulum membrane ; Peripheral membrane protein : O75340
• Total number of polymer chains: 8
• Total formula weight: 159450.46

Authors

Suzuki, H.,Kawasaki, M.,Kakiuchi, T.,Shibata, H.,Wakatsuki, S.,Maki, M. (deposition date: 2008-09-01, release date: 2008-11-04, Last modification date: 2023-11-01)

Primary citation

Suzuki, H.,Kawasaki, M.,Kakiuchi, T.,Shibata, H.,Wakatsuki, S.,Maki, M.
Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2
ACTA CRYSTALLOGR.,SECT.F, 64:974-977, 2008

PubMed Abstract: ALG-2 (apoptosis-linked gene 2) is an apoptosis-linked calcium-binding protein with five EF-hand motifs in the C-terminal region. N-terminally truncated ALG-2 (des3-23ALG-2) was crystallized by the vapour-diffusion method in buffer consisting of either 50 mM MES pH 6.5, 12.5%(v/v) 2-propanol and 150 mM calcium acetate or 100 mM MES pH 6.0, 15%(v/v) ethanol and 200 mM zinc acetate. Crystals of the Ca(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.8, b = 154.4, c = 237.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.1 A resolution. Crystals of the Zn(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.8, b = 147.5, c = 230.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.3 A resolution. The structures of the Ca(2+)-bound form and the Zn(2+)-bound form were solved by the molecular-replacement method. Although both crystals contained eight ALG-2 molecules per asymmetric unit, the metal-ion locations and octameric arrangements were found to be significantly different.

PubMed: 18997320
DOI: 10.1107/S1744309108030297

Experimental method

X-RAY DIFFRACTION (3.1 Å)