2K8A
Solution structure of a novel Ubiquitin-binding domain from Human PLAA (PFUC, Gly76-Pro77 trans isomer)
Summary for 2K8A
| Entry DOI | 10.2210/pdb2k8a/pdb |
| Related | 2K89 2K8B 2K8C |
| NMR Information | BMRB: 16818 |
| Descriptor | Phospholipase A-2-activating protein (1 entity in total) |
| Functional Keywords | ubiquitin binding, wd repeat, protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9032.01 |
| 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 Cited by 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: 19423704DOI: 10.1074/jbc.M109.009126 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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