7Q3A

Crystal structure of MAB_4324 a tandem repeat GNAT from Mycobacterium abscessus

Summary for 7Q3A

• Entry DOI: 10.2210/pdb7q3a/pdb
• Descriptor: Putative acetyltransferase, GNAT, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, COENZYME A, ... (9 entities in total)
• Functional Keywords: n-acetyltransferase, acetyl-coa, transferase
• Biological source: Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus)
• Total number of polymer chains: 2
• Total formula weight: 83453.84

Authors

Blaise, M.,Alsarraf, M.A.B. (deposition date: 2021-10-27, release date: 2022-05-04, Last modification date: 2024-06-19)

Primary citation

Alsarraf, H.M.A.B.,Ung, K.L.,Johansen, M.D.,Dimon, J.,Olieric, V.,Kremer, L.,Blaise, M.
Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N-acetyltransferase.
Febs Lett., 596:1516-1532, 2022

PubMed Abstract: Mycobacterium abscessus is a pathogenic non-tuberculous mycobacterium that possesses an intrinsic drug resistance profile. Several N-acetyltransferases mediate drug resistance and/or participate in M. abscessus virulence. Mining the M. abscessus genome has revealed genes encoding additional N-acetyltransferases whose functions remain uncharacterized, among them MAB_4324c. Here, we showed that the purified MAB_4324c protein is a N-acetyltransferase able to acetylate small polyamine substrates. The crystal structure of MAB_4324c was solved at high resolution in complex with its cofactor, revealing the presence of two GCN5-related N-acetyltransferase domains and a cryptic binding site for NADPH. Genetic studies demonstrate that MAB_4324c is not essential for in vitro growth of M. abscessus; however, overexpression of the protein enhanced the uptake and survival of M. abscessus in THP-1 macrophages.

PubMed: 35470425
DOI: 10.1002/1873-3468.14360

Experimental method

X-RAY DIFFRACTION (2 Å)