7DNP

Structure of Brucella abortus SagA

Summary for 7DNP

• Entry DOI: 10.2210/pdb7dnp/pdb
• Descriptor: Secretion activator protein, hypothetical, (2R)-2-[[(2S)-2-[[(2R)-2-[(2R,3S,4R,5R,6S)-5-acetamido-3-[(2S,3R,4R,5S,6R)-3-acetamido-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-2-yl]oxy-2-(hydroxymethyl)-6-oxidanyl-oxan-4-yl]oxypropanoyl]amino]propanoyl]amino]pentanedioic acid (3 entities in total)
• Functional Keywords: saga, muramidase, brucella abortus, t4ss, hydrolase
• Biological source: Brucella abortus bv. 1 str. 9-941
• Total number of polymer chains: 1
• Total formula weight: 20477.25

Authors

Hyun, Y.,Ha, N.-C. (deposition date: 2020-12-10, release date: 2021-06-23, Last modification date: 2024-05-29)

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 (2 Å)