Sandbox Reserved 1588

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Revision as of 15:53, 30 November 2019

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).

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FhaC membrane transporter

1 Function
2 Disease
3 Relevance
4 Structural highlights

Function

FhaC membrane transporter is a protein in the Omp85 family. It involves two polypeptide-transport associated (POTRA) domains, which are involved in substrate recognition. This protein's main function is to aid in FHA, or filamentous hemagglutinin, secretion. This is carried out by a two-partner secretion system, where FhaC is the translocase and FHA is the substrate. The beta-barrel conformation provides the pore for FHA transport through the membrane of the cell. The substrate is involved in a competitive mechanism with a linker protein, H1 helix, that normally rests inside of the barrel to block transport. This helix interacts weakly with the POTRA2 domain, to sit inside the pore. When the substrate (FHA) arrives at the transport site, it competes with the linker protein for the interaction with the POTRA2 domain. This pushes the H1 helix out, allowing the pore to be used for FHA secretion. ^[1]

Disease

Relevance

Structural highlights

The structure of this protein is a wide, round barrel shape, with two POTRA domains just below the barrel, and a linker protein at the N-terminus, the H1 helix. An important feature of this protein’s structure is the “lid-lock” formation with the interaction of two signature motifs, one in the inner barrel wall, and one at the tip of the L6 loop. The H1 helix acts as a plug for the membrane transporter by traversing the entire length of the barrel, sitting inside the pore, blocking activity through the pore. This happens in the absence of substrates, so in these conditions, the barrel is “inactive.” H1 can be displaced by substrate binding. When displaced, the H1 helix rests flexibly on the periplasmic face membrane near the two POTRA domains. The L6 loop is required for channel stability and FHA secretion. The motif in the L6 loop interacts with the motif on the inner wall through close spatial contact and through salt bridges. This ensures the lid-lock formation that is necessary for stability and aids in FHA secretion through the insertion site which is also on the L6 loop.

References

↑ Maier T, Clantin B, Gruss F, Dewitte F, Delattre AS, Jacob-Dubuisson F, Hiller S, Villeret V. Conserved Omp85 lid-lock structure and substrate recognition in FhaC. Nat Commun. 2015 Jun 10;6:7452. doi: 10.1038/ncomms8452. PMID:26058369 doi:http://dx.doi.org/10.1038/ncomms8452

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Sandbox Reserved 1588

From Proteopedia

Revision as of 15:53, 30 November 2019

FhaC membrane transporter

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Structural highlights

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@@ Line 11: / Line 11: @@
 == Structural highlights ==
+The structure of this protein is a wide, round barrel shape, with two POTRA domains just below the barrel, and a linker protein at the N-terminus, the H1 helix. An important feature of this protein’s structure is the “lid-lock” formation with the interaction of two signature motifs, one in the inner barrel wall, and one at the tip of the L6 loop.
+The H1 helix acts as a plug for the membrane transporter by traversing the entire length of the barrel, sitting inside the pore, blocking activity through the pore. This happens in the absence of substrates, so in these conditions, the barrel is “inactive.” H1 can be displaced by substrate binding. When displaced, the H1 helix rests flexibly on the periplasmic face membrane near the two POTRA domains.
+The L6 loop is required for channel stability and FHA secretion. The motif in the L6 loop interacts with the motif on the inner wall through close spatial contact and through salt bridges. This ensures the lid-lock formation that is necessary for stability and aids in FHA secretion through the insertion site which is also on the L6 loop.