3AAK

Crystal structure of Zn2+-bound form of des3-20ALG-2F122A

Summary for 3AAK

• Entry DOI: 10.2210/pdb3aak/pdb
• Related: 1HQV 2ZN8 2ZN9 2ZND 2ZNE 2ZRS 2ZRT 3AAJ
• Descriptor: Programmed cell death protein 6, ZINC ION (3 entities in total)
• Functional Keywords: penta-ef-hand protein, calcium-binding protein, apoptosis, endoplasmic reticulum
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane ; Peripheral membrane protein : O75340
• Total number of polymer chains: 1
• Total formula weight: 20278.62

Authors

Inuzuka, T.,Suzuki, H.,Kawasaki, M.,Shibata, H.,Wakatsuki, S.,Maki, M. (deposition date: 2009-11-19, release date: 2010-09-08, Last modification date: 2023-11-01)

Primary citation

Inuzuka, T.,Suzuki, H.,Kawasaki, M.,Shibata, H.,Wakatsuki, S.,Maki, M.
Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition
Bmc Struct.Biol., 10:25-25, 2010

PubMed Abstract: ALG-2 (a gene product of PDCD6) belongs to the penta-EF-hand (PEF) protein family and Ca2+-dependently interacts with various intracellular proteins including mammalian Alix, an adaptor protein in the ESCRT system. Our previous X-ray crystal structural analyses revealed that binding of Ca2+ to EF3 enables the side chain of R125 to move enough to make a primary hydrophobic pocket (Pocket 1) accessible to a short fragment of Alix. The side chain of F122, facing a secondary hydrophobic pocket (Pocket 2), interacts with the Alix peptide. An alternatively spliced shorter isoform, designated ALG-2DeltaGF122, lacks Gly121Phe122 and does not bind Alix, but the structural basis of the incompetence has remained to be elucidated.

PubMed: 20691033
DOI: 10.1186/1472-6807-10-25

Experimental method

X-RAY DIFFRACTION (2.7 Å)