7DPY

Structure of Brucella abortus PhiA

Summary for 7DPY

• Entry DOI: 10.2210/pdb7dpy/pdb
• Descriptor: Brucella Abortus PhiA (2 entities in total)
• Functional Keywords: t4ss, lysozyme inhibitor, plic, unknown function
• Biological source: Brucella abortus bv. 1 str. 9-941
• Total number of polymer chains: 2
• Total formula weight: 24535.08

Authors

Hyun, Y.,Ha, N.-C. (deposition date: 2020-12-22, release date: 2021-06-23, Last modification date: 2024-11-13)

Primary citation

Hyun, Y.,Baek, Y.,Lee, C.,Ki, N.,Ahn, J.,Ryu, S.,Ha, N.C.
Structure and Function of the Autolysin SagA in the Type IV Secretion System of Brucella abortus .
Mol.Cells, 44:517-528, 2021

PubMed Abstract: A recent genetic study with revealed the secretion activator gene A (SagA) as an autolysin component creating pores in the peptidoglycan (PGN) layer for the type IV secretion system (T4SS) and peptidoglycan hydrolase inhibitor A (PhiA) as an inhibitor of SagA. In this study, we determined the crystal structures of both SagA and PhiA. Notably, the SagA structure contained a PGN fragment in a space between the N- and C-terminal domains, showing the substrate-dependent hinge motion of the domains. The purified SagA fully hydrolyzed the meso-diaminopimelic acid (DAP)-type PGN, showing a higher activity than hen egg-white lysozyme. The PhiA protein exhibiting tetrameric assembly failed to inhibit SagA activity in our experiments. Our findings provide implications for the molecular basis of the SagA-PhiA system of . The development of inhibitors of SagA would further contribute to controlling brucellosis by attenuating the function of T4SS, the major virulence factor of .

PubMed: 34112742
DOI: 10.14348/molcells.2021.0011

Experimental method

X-RAY DIFFRACTION (1.8 Å)