The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions.
The ErbB-3 receptor binding protein (Ebp1) is a member of the proliferation-associated 2G4 (PA2G4) family implicated in regulation of cell growth and differentiation. Here, we report the crystal structure of the human Ebp1 at 1.6 A resolution. The protein has the conserved pita bread fold of methionine aminopeptidases, but without the characteristic enzymatic activity. Moreover, Ebp1 is known to interact with a number of proteins and RNAs involved in either transcription regulation or translation control. The structure provides insights in how Ebp1 discriminates between its different interaction partners.
Kowalinski
Eva
E
Heidelberg University Biochemistry Center (BZH), INF 328, D-69120 Heidelberg, Germany.
Bange
Gert
G
Bradatsch
Bettina
B
Hurt
Ed
E
Wild
Klemens
K
Sinning
Irmgard
I
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000626:Aminopeptidases / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D063208:Methionyl Aminopeptidases; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012341:RNA, Ribosomal, 5S / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D048868:Adaptor Proteins, Signal Transducing; C101633:PA2G4 protein, human; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases