2K8B

Solution structure of PLAA family ubiquitin binding domain (PFUC) cis isomer in complex with ubiquitin

Summary for 2K8B

• Entry DOI: 10.2210/pdb2k8b/pdb
• Related: 2K89 2K8A 2K8C
• Descriptor: Ubiquitin, Phospholipase A-2-activating protein (2 entities in total)
• Functional Keywords: ubiquitin in complex with pfuc cis isomer, cytoplasm, nucleus, phosphoprotein, ubl conjugation, wd repeat, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 17608.84

Authors

Fu, Q.S.,Zhou, C.J.,Gao, H.C.,Lin, D.H.,Hu, H.Y. (deposition date: 2008-09-04, release date: 2009-05-05, Last modification date: 2024-05-22)

Primary citation

Fu, Q.S.,Zhou, C.J.,Gao, H.C.,Jiang, Y.J.,Zhou, Z.R.,Hong, J.,Yao, W.M.,Song, A.X.,Lin, D.H.,Hu, H.Y.
Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein.
J.Biol.Chem., 284:19043-19052, 2009

PubMed Abstract: Ubiquitin (Ub) is an essential modifier conserved in all eukaryotes from yeast to human. Phospholipase A(2)-activating protein (PLAA), a mammalian homolog of yeast DOA1/UFD3, has been proposed to be able to bind with Ub, which plays important roles in endoplasmic reticulum-associated degradation, vesicle formation, and DNA damage response. We have identified a core domain from the PLAA family ubiquitin-binding region of human PLAA (residues 386-465, namely PFUC) that can bind Ub and elucidated its solution structure and Ub-binding mode by NMR approaches. The PFUC domain possesses equal population of two conformers in solution by cis/trans-isomerization, whereas the two isomers exhibit almost equivalent Ub binding abilities. This domain structure takes a novel fold consisting of four beta-strands and two alpha-helices, and the Ub-binding site on PFUC locates in the surface of alpha2-helix, which is to some extent analogous to those of UBA, CUE, and UIM domains. This study provides structural basis and biochemical information for Ub recognition of the novel PFU domain from a PLAA family protein that may connect ubiquitination and degradation in endoplasmic reticulum-associated degradation.

PubMed: 19423704
DOI: 10.1074/jbc.M109.009126

Experimental method

SOLUTION NMR