1gv4: Difference between revisions
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|PDB= 1gv4 |SIZE=350|CAPTION= <scene name='initialview01'>1gv4</scene>, resolution 2.00Å | |PDB= 1gv4 |SIZE=350|CAPTION= <scene name='initialview01'>1gv4</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv4 OCA], [http://www.ebi.ac.uk/pdbsum/1gv4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gv4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Alzari, P M.]] | [[Category: Alzari, P M.]] | ||
[[Category: Mate, M J.]] | [[Category: Mate, M J.]] | ||
[[Category: apoptosi]] | [[Category: apoptosi]] | ||
[[Category: fad]] | [[Category: fad]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:59 2008'' | ||
Revision as of 17:52, 30 March 2008
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| 1gv4, resolution 2.00Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | FAD | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MURINE APOPTOSIS-INDUCING FACTOR (AIF)
Overview
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.
About this Structure
1GV4 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the mouse apoptosis-inducing factor AIF., Mate MJ, Ortiz-Lombardia M, Boitel B, Haouz A, Tello D, Susin SA, Penninger J, Kroemer G, Alzari PM, Nat Struct Biol. 2002 Jun;9(6):442-6. PMID:11967568
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