2023
DOI: 10.1038/s41467-023-36590-1
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Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter

Abstract: In bacteria and archaea, tripartite ATP-independent periplasmic (TRAP) transporters uptake essential nutrients. TRAP transporters receive their substrates via a secreted soluble substrate-binding protein. How a sodium ion-driven secondary active transporter is strictly coupled to a substrate-binding protein is poorly understood. Here we report the cryo-EM structure of the sialic acid TRAP transporter SiaQM from Photobacterium profundum at 2.97 Å resolution. SiaM comprises a “transport” domain and a “scaffold” … Show more

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Cited by 25 publications
(46 citation statements)
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“…for alignment = ~0.2 Å, Figure 2a,b). This is the same conformation as the previous megabody-bound PpSiaQM structures in amphipol and a nanodisc (33) and also the same as the recently reported lower resolution (4.7 Å) megabody-bound HiSiaQM structure in a nanodisc (27). Three-dimensional variability analysis (3DVA) (34)…”
Section: (Insert Figure 2)supporting
confidence: 87%
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“…for alignment = ~0.2 Å, Figure 2a,b). This is the same conformation as the previous megabody-bound PpSiaQM structures in amphipol and a nanodisc (33) and also the same as the recently reported lower resolution (4.7 Å) megabody-bound HiSiaQM structure in a nanodisc (27). Three-dimensional variability analysis (3DVA) (34)…”
Section: (Insert Figure 2)supporting
confidence: 87%
“…We determined the homodimeric (2QM) structure of HiSiaQM using single particle cryo-electron microscopy, the first structure of a fused TRAP transporter at near atomic resolution (2.99 Å, with local resolution extending to ~2.2 Å), which reveals new details of the transport mechanism. The structure, combined with functional and biophysical data, supports the hypothesis that HiSiaQM operates using the 'elevator-with-an-operator' mechanism that we proposed for TRAP transporters (33).…”
Section: Introductionsupporting
confidence: 81%
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“…Bacteria rely on specialized Neu5Ac transporters within their cytosolic membranes, and four distinct classes of Neu5Ac transporters have been identified: sodium solute symporters (SSS) (North et al, 2018), major facilitator superfamily (MFS), ATP-binding cassette (ABC), and tripartite ATP-independent periplasmic (TRAP) transporters (Davies et al, 2023;Severi et al, 2021). Of particular interest are TRAP transporters that manifest as two-or three-component systems consisting of a substrate-binding protein (SiaP) and transmembrane protein (SiaQM) (Rosa et al, 2018).…”
Section: Introductionmentioning
confidence: 99%
“…Similarly, PpSiaQM has a structure with 16 transmembrane helices (Davies et al, 2023). Based on these structures, TRAP transporters are postulated to employ an elevator-type mechanism to transport substrates from the periplasm to the cytoplasm.…”
Section: Introductionmentioning
confidence: 99%