7BY1

Crystal structure of GCN5 PCAF N-terminal domain

Summary for 7BY1

• Entry DOI: 10.2210/pdb7by1/pdb
• Descriptor: Histone acetyltransferase KAT2A, ZINC ION (3 entities in total)
• Functional Keywords: ubiquitin ligase, unknown function
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 73365.82

Authors

Hibi, R.,Toma-Fukai, S.,Shimizu, T. (deposition date: 2020-04-21, release date: 2020-08-26, Last modification date: 2024-03-27)

Primary citation

Toma-Fukai, S.,Hibi, R.,Naganuma, T.,Sakai, M.,Saijo, S.,Shimizu, N.,Matsumoto, M.,Shimizu, T.
Crystal structure of GCN5 PCAF N-terminal domain reveals atypical ubiquitin ligase structure.
J.Biol.Chem., 295:14630-14639, 2020

PubMed Abstract: General control nonderepressible 5 (GCN5, also known as Kat2a) and p300/CBP-associated factor (PCAF, also known as Kat2b) are two homologous acetyltransferases. Both proteins share similar domain architecture consisting of a PCAF N-terminal (PCAF_N) domain, acetyltransferase domain, and a bromodomain. PCAF also acts as a ubiquitin E3 ligase whose activity is attributable to the PCAF_N domain, but its structural aspects are largely unknown. Here, we demonstrated that GCN5 exhibited ubiquitination activity in a similar manner to PCAF and its activity was supported by the ubiquitin-conjugating enzyme UbcH5. Moreover, we determined the crystal structure of the PCAF_N domain at 1.8 Å resolution and found that PCAF_N domain folds into a helical structure with a characteristic binuclear zinc region, which was not predicted from sequence analyses. The zinc region is distinct from known E3 ligase structures, suggesting this region may form a new class of E3 ligase. Our biochemical and structural study provides new insight into not only the functional significance of GCN5 but also into ubiquitin biology.

PubMed: 32820047
DOI: 10.1074/jbc.RA120.013431

Experimental method

X-RAY DIFFRACTION (1.8 Å)