6drq | pdb_00006drq

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

spinqualitylabelsall models 6drq, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6drq is a 1 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR Gene: LH57_18085 (MYCTU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The SecA2 protein export system is critical for the virulence of Mycobacterium tuberculosis. However, the mechanism of this export pathway remains unclear. Through a screen for suppressors of a secA2 mutant, we identified a new player in the mycobacterial SecA2 pathway that we named SatS for SecA2 (two) Suppressor. In M. tuberculosis, 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 M. tuberculosis pathogenesis and in expanding our appreciation of the diversity among chaperones and protein export systems. Mycobacterium tuberculosis SatS is a chaperone for the SecA2 protein export pathway.,Miller BK, Hughes R, Ligon LS, Rigel NW, Malik S, Anjuwon-Foster BR, Sacchettini JC, Braunstein M Elife. 2019 Jan 3;8. pii: 40063. doi: 10.7554/eLife.40063. PMID:30604681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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