6B0U

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with a Lys-containing peptide

Summary for 6B0U

• Entry DOI: 10.2210/pdb6b0u/pdb
• Descriptor: N-acetyltransferase Eis, Synthetic peptide ATKAPAKKA, COENZYME A (3 entities in total)
• Functional Keywords: histone acetylation, aminoglycoside, drug resistance, tuberculosis, acetylation, transferase
• Biological source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); More
• Total number of polymer chains: 5
• Total formula weight: 145692.54

Authors

Biswas, T.,Pang, A.H.,Garneau-Tsodikova, S.,Tsodikov, O.V. (deposition date: 2017-09-15, release date: 2018-01-31, Last modification date: 2024-11-06)

Primary citation

Green, K.D.,Biswas, T.,Pang, A.H.,Willby, M.J.,Reed, M.S.,Stuchlik, O.,Pohl, J.,Posey, J.E.,Tsodikov, O.V.,Garneau-Tsodikova, S.
Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.
Biochemistry, 57:781-790, 2018

PubMed Abstract: Bacterial nucleoid-associated proteins (NAPs) are critical to genome integrity and chromosome maintenance. Post-translational modifications of bacterial NAPs appear to function similarly to their better studied mammalian counterparts. The histone-like NAP HupB from Mycobacterium tuberculosis (Mtb) was previously observed to be acetylated by the acetyltransferase Eis, leading to genome reorganization. We report biochemical and structural aspects of acetylation of HupB by Eis. We also found that the SirT-family NAD-dependent deacetylase Rv1151c from Mtb deacetylated HupB in vitro and characterized the deacetylation kinetics. We propose that activities of Eis and Rv1151c could regulate the acetylation status of HupB to remodel the mycobacterial chromosome in response to environmental changes.

PubMed: 29345920
DOI: 10.1021/acs.biochem.7b01089

Experimental method

X-RAY DIFFRACTION (2.8 Å)