6BS3

Crystal structure of ADP-bound bacterial Get3-like A and B in Mycobacterium tuberculosis

Summary for 6BS3

• Entry DOI: 10.2210/pdb6bs3/pdb
• Descriptor: Putative ATPase Rv3679, Anion transporter, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: complex, unknown function
• Biological source: Mycobacterium tuberculosis H37Rv; More
• Total number of polymer chains: 2
• Total formula weight: 79464.05

Authors

Li, H.,Hu, K.,Kovach, A. (deposition date: 2017-12-01, release date: 2019-05-15, Last modification date: 2024-03-13)

Primary citation

Hu, K.,Jordan, A.T.,Zhang, S.,Dhabaria, A.,Kovach, A.,Rangel, M.V.,Ueberheide, B.,Li, H.,Darwin, K.H.
Characterization of Guided Entry of Tail-Anchored Proteins 3 Homologues in Mycobacterium tuberculosis.
J.Bacteriol., 201:-, 2019

PubMed Abstract: We characterized an operon in , Rv3679-Rv3680, in which each open reading frame is annotated to encode "anion transporter ATPase" homologues. Using structure prediction modeling, we found that Rv3679 and Rv3680 more closely resemble the uided ntry of ail-anchored proteins (Get3) chaperone in eukaryotes. Get3 delivers proteins into the membranes of the endoplasmic reticulum and is essential for the normal growth and physiology of some eukaryotes. We sought to characterize the structures of Rv3679 and Rv3680 and test if they have a role in pathogenesis. We solved crystal structures of the nucleotide-bound Rv3679-Rv3680 complex at 2.5 to 3.2 Å and show that while it has some similarities to Get3 and ArsA, there are notable differences, including that these proteins are unlikely to be involved in anion transport. Deletion of both genes did not reveal any conspicuous growth defects or in mice. Collectively, we identified a new class of proteins in bacteria with similarity to Get3 complexes, the functions of which remain to be determined. Numerous bacterial species encode proteins predicted to have similarity with Get3- and ArsA-type anion transporters. Our studies provide evidence that these proteins, which we named BagA and BagB, are unlikely to be involved in anion transport. In addition, BagA and BagB are conserved in all mycobacterial species, including the causative agent of leprosy, which has a highly decayed genome. This conservation suggests that BagAB constitutes a part of the core mycobacterial genome and is needed for some yet-to-be-determined part of the life cycle of these organisms.

PubMed: 31036728
DOI: 10.1128/JB.00159-19

Experimental method

X-RAY DIFFRACTION (2.3 Å)