7CZ2

The complex structure of MSMEG_1954-ADP from Mycobacterium smegmatis

Summary for 7CZ2

• Entry DOI: 10.2210/pdb7cz2/pdb
• Descriptor: ABC1 family protein, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: antibiotic binding, adp binding, transport protein
• Biological source: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
• Total number of polymer chains: 1
• Total formula weight: 48514.60

Authors

Zhang, Q.,Rao, Z.H. (deposition date: 2020-09-07, release date: 2021-12-08, Last modification date: 2023-11-29)

Primary citation

Zhang, Q.,Liu, X.,Liu, H.,Zhang, B.,Yang, H.,Mi, K.,Guddat, L.W.,Rao, Z.
Conformational Changes in a Macrolide Antibiotic Binding Protein From Mycobacterium smegmatis Upon ADP Binding.
Front Microbiol, 12:780954-780954, 2021

PubMed Abstract: Rv3197 (MABP-1), a non-canonical ABC protein in , has ATPase activity and confers inducible resistance to the macrolide family of antibiotics. Here we have shown that MSMEG_1954, the homolog of Rv3197 in , has a similar function of conferring macrolide resistance. Crystal structures of apo-MSMEG_1954 (form1 and form 2) and MSMEG_1954 in complex with ADP have been determined. These three structures show that MSMEG_1954 has at least two different conformations we identify as closed state (MSMEG_1954-form 1) and open state (MSMEG_1954-form 2 and MSMEG_1954-ADP). Structural superimposition shows that the MSMEG_1954-form 2 and MSMEG_1954-ADP complex have similar conformation to that observed for MABP-1 and MABP-1-erythromicin complex structure. However, the antibiotic binding pocket in MSMEG_1954-form 1 is completely blocked by the N-terminal accessory domain. When bound by ADP, the N-terminal accessory domain undergoes conformational change, which results in the open of the antibiotic binding pocket. Because of the degradation of N terminal accessory domain in MSMSG_1954-form 2, it is likely to represent a transitional state between MSMEG_1954-form 1 and MSMEG_1954-ADP complex structure.

PubMed: 34956144
DOI: 10.3389/fmicb.2021.780954

Experimental method

X-RAY DIFFRACTION (1.8 Å)