6DRQ

The crystal structure of SatS c-terminal domain in complex with bromine

Summary for 6DRQ

• Entry DOI: 10.2210/pdb6drq/pdb
• Descriptor: Primosomal protein, BROMIDE ION (3 entities in total)
• Functional Keywords: seca2, protein export, chaperone, structural genomics, psi-2, protein structure initiative, tb structural genomics consortium, tbsgc
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 20860.52

Authors

Hughes, R.C.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2018-06-12, release date: 2019-01-23, Last modification date: 2024-03-13)

Primary citation

Miller, B.K.,Hughes, R.,Ligon, L.S.,Rigel, N.W.,Malik, S.,Anjuwon-Foster, B.R.,Sacchettini, J.C.,Braunstein, M.
Mycobacterium tuberculosisSatS is a chaperone for the SecA2 protein export pathway.
Elife, 8:-, 2019

PubMed Abstract: The SecA2 protein export system is critical for the virulence of . However, the mechanism of this export pathway remains unclear. Through a screen for suppressors of a mutant, we identified a new player in the mycobacterial SecA2 pathway that we named SatS for ec2 (wo) uppressor. In , SatS is required for the export of a subset of SecA2 substrates and for growth in macrophages. We further identify a role for SatS as a protein export chaperone. SatS exhibits multiple properties of a chaperone, including the ability to bind to and protect substrates from aggregation. Our structural studies of SatS reveal a distinct combination of a new fold and hydrophobic grooves resembling preprotein-binding sites of the SecB chaperone. These results are significant in better defining a molecular pathway for pathogenesis and in expanding our appreciation of the diversity among chaperones and protein export systems.

PubMed: 30604681
DOI: 10.7554/eLife.40063

Experimental method

X-RAY DIFFRACTION (2.3 Å)