1GV4
Murine apoptosis-inducing factor (AIF)
Summary for 1GV4
Entry DOI | 10.2210/pdb1gv4/pdb |
Descriptor | PROGRAMED CELL DEATH PROTEIN 8, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
Functional Keywords | oxidoreductase, flavoprotein, fad, nuclear protein, apoptosi |
Biological source | MUS MUSCULUS |
Cellular location | Mitochondrion intermembrane space: Q9Z0X1 |
Total number of polymer chains | 2 |
Total formula weight | 116713.95 |
Authors | Mate, M.J.,Alzari, P.M. (deposition date: 2002-02-05, release date: 2002-04-26, Last modification date: 2023-12-13) |
Primary citation | Mate, M.J.,Ortiz-Lombardia, M.,Alzari, P.M.,Boitel, B.,Haouz, A.,Tello, D.,Susin, S.A.,Penninger, J.,Kroemer, G.,Alzari, P.M. The Crystal Structure of the Mouse Apoptosis-Inducing Factor Aif Nat.Struct.Biol., 9:442-, 2002 Cited by PubMed Abstract: Mitochondria play a key role in apoptosis due to their capacity to release potentially lethal proteins. One of these latent death factors is cytochrome c, which can stimulate the proteolytic activation of caspase zymogens. Another important protein is apoptosis-inducing factor (AIF), a flavoprotein that can stimulate a caspase-independent cell-death pathway required for early embryonic morphogenesis. Here, we report the crystal structure of mouse AIF at 2.0 A. Its active site structure and redox properties suggest that AIF functions as an electron transferase with a mechanism similar to that of the bacterial ferredoxin reductases, its closest evolutionary homologs. However, AIF structurally differs from these proteins in some essential features, including a long insertion in a C-terminal beta-hairpin loop, which may be related to its apoptogenic functions. PubMed: 11967568DOI: 10.1038/NSB793 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report