1Y02

Crystal Structure of a FYVE-type domain from caspase regulator CARP2

Summary for 1Y02

• Entry DOI: 10.2210/pdb1y02/pdb
• Descriptor: FYVE-RING finger protein SAKURA, ZINC ION (3 entities in total)
• Functional Keywords: carp2, fyve, zinc-binding module, phosphoinositide binding, caspase regulation, metal binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q8WZ73
• Total number of polymer chains: 1
• Total formula weight: 13724.52

Authors

Tibbetts, M.D.,Gu, L.,Shiozaki, E.N.,Shi, Y. (deposition date: 2004-11-14, release date: 2004-12-28, Last modification date: 2024-02-14)

Primary citation

Tibbetts, M.D.,Shiozaki, E.N.,Gu, L.,McDonald, E.R.,El-Deiry, W.S.,Shi, Y.
Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2.
STRUCTURE, 12:2257-2263, 2004

PubMed Abstract: The caspase-associated ring proteins (CARP1 and CARP2) are distinguished from other caspase regulators by the presence of a FYVE-type zinc finger domain. FYVE-type domains are divided into two known classes: FYVE domains that specifically bind to phosphatidylinositol 3-phosphate in lipid bilayers and FYVE-related domains of undetermined function. Here, we report the crystal structure of the N-terminal region of CARP2 (44-139) including the FYVE-type domain and its associated helical bundle at 1.7 A resolution. The structure reveals a cramped phosphoinositide binding pocket and a blunted membrane insertion loop. These structural features indicate that the domain is not optimized to bind to phosphoinositides or insert into lipid bilayers. The CARP2 FYVE-like domain thus defines a third subfamily of FYVE-type domains that are functionally and structurally distinct. Structural analyses provide insights into the possible function of this unique subfamily of FYVE-type domains.

PubMed: 15576038
DOI: 10.1016/j.str.2004.10.007

Experimental method

X-RAY DIFFRACTION (1.8 Å)