Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form II

Masuda, Shoko; Murakami, Katsuhiko; Wang, S.; Olson, Connor A.; Donigian, Jill R.; Leon, F.; Darst, Seth A.; Campbell, Elizabeth A.

doi:10.2210/pdb1th8/pdb

2004

DOI: 10.2210/pdb1th8/pdb

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Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form II

Shoko Masuda¹,

Katsuhiko Murakami²,

S. Wang³

et al.

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2020

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Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

Kolich

Chang

Coudray

et al. 2020

Preprint

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ABC transporters facilitate the movement of a diverse array of molecules across cellular membranes, using power from ATP hydrolysis. While the overall mechanism of the transport cycle has been characterized in detail for several important members of this transporter family, it is less well understood how the activity of ABC transporters is regulated in the cell post-translationally. Here we report the X-ray crystal structure of MlaFB from E. coli, an ABC nucleotide binding domain (MlaF) in complex with its putative regulatory subunit (MlaB). MlaFB constitutes the cytoplasmic portion of the larger MlaFEDB ABC transporter complex, which drives phospholipid transport across the bacterial envelope and is important for maintaining the integrity of the outer membrane barrier. Our data show that the regulatory subunit MlaB, a STAS domain protein, binds to the nucleotide binding domain and is required for its stability. Our structure also implicates a unique Cterminal tail of the ABC subunit, MlaF, in self-dimerization. Both the C-terminal tail of MlaF and the interaction with MlaB are required for the proper assembly of the MlaFEDB complex and its function in cells. This work leads to a new model for how the activity of an important bacterial lipid transporter may be regulated by small binding proteins, and raises the possibility that similar regulatory mechanisms may exist more broadly across the ABC transporter family, from bacteria to humans.

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Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

Kolich

Chang

Coudray

et al. 2020

Preprint

View full text Add to dashboard Cite

show abstract

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Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form II

Cited by 1 publication

References 0 publications

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

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