4ql0

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(Difference between revisions)

Revision as of 11:42, 15 December 2016

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

Structural highlights

4ql0 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , ,
Related:	4qky, 2qdz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FHAC_BORPE] Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin (FHA).^[1]

Publication Abstract from PubMed

Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded beta-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 A resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1.

Conserved Omp85 lid-lock structure and substrate recognition in FhaC.,Maier T, Clantin B, Gruss F, Dewitte F, Delattre AS, Jacob-Dubuisson F, Hiller S, Villeret V Nat Commun. 2015 Jun 10;6:7452. doi: 10.1038/ncomms8452. PMID:26058369^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hodak H, Clantin B, Willery E, Villeret V, Locht C, Jacob-Dubuisson F. Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol Microbiol. 2006 Jul;61(2):368-82. Epub 2006 Jun 12. PMID:16771844 doi:10.1111/j.1365-2958.2006.05242.x
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ql0"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)==
 <StructureSection load='4ql0' size='340' side='right' caption='[[4ql0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qky|4qky]], [[2qdz|2qdz]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ql0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ql0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ql0 OCA], [http://pdbe.org/4ql0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ql0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ql0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ql0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-Widespread in Gram-negative bacteria, the two-partner secretion (TPS) pathway mediates the secretion of large, beta-helical 'TpsA' proteins with various functions. TpsA proteins harbour a conserved, N-proximal TPS domain essential for secretion. TpsB transporters specifically recognize their TpsA partners in the periplasm and mediate their translocation across the outer membrane through a hydrophilic channel. The FHA/FhaC pair of Bordetella pertussis represents a model TPS system. FhaC is composed of a beta barrel preceded by two periplasmic POTRA domains in tandem. Here we show that both POTRAs are involved in FHA recognition. Surface plasmon resonance analyses indicated an interaction of micromolar affinity between the POTRAs and the TPS domain with fast association and dissociation steps, consistent with the transient character of this interaction in vivo. Major interaction sites in POTRAs correspond to hydrophobic grooves formed by a beta sheet edge and the flanking alpha helix, well-suited to accommodate extended, amphipathic strands of the substrate and consistent with beta augmentation. The initial recruitment of the TPS domain to POTRAs appears to be facilitated by electrostatic attractions. A domain corresponding to the first part of the repeat-rich central region of FHA is also recognized by the POTRAs, suggesting successive interactions in the course of secretion.
+Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded beta-barrel pore and two signature motifs located on the inner barrel wall and at the tip of the extended L6 loop. The observation of two distinct conformations of the L6 loop in the available Omp85 structures previously suggested a functional role of conformational changes in L6 in the Omp85 mechanism. Here we present a 2.5 A resolution structure of a variant of the Omp85 secretion protein FhaC, in which the two signature motifs interact tightly and form the conserved 'lid lock'. Reanalysis of previous structural data shows that L6 adopts the same, conserved resting state position in all available Omp85 structures. The FhaC variant structure further reveals a competitive mechanism for the regulation of substrate binding mediated by the linker to the N-terminal plug helix H1.
-Substrate recognition by the POTRA domains of TpsB transporter FhaC.,Delattre AS, Saint N, Clantin B, Willery E, Lippens G, Locht C, Villeret V, Jacob-Dubuisson F Mol Microbiol. 2011 Jul;81(1):99-112. doi: 10.1111/j.1365-2958.2011.07680.x. Epub, 2011 Jun 14. PMID:21542859<ref>PMID:21542859</ref>
+Conserved Omp85 lid-lock structure and substrate recognition in FhaC.,Maier T, Clantin B, Gruss F, Dewitte F, Delattre AS, Jacob-Dubuisson F, Hiller S, Villeret V Nat Commun. 2015 Jun 10;6:7452. doi: 10.1038/ncomms8452. PMID:26058369<ref>PMID:26058369</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ql0" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ql0

From Proteopedia

Revision as of 11:42, 15 December 2016

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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