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Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85

Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85
Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85
Proteins of the Omp85 family are conserved in all kingdoms of life. They mediate protein transport across or protein insertion into membranes and reside in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. Omp85 proteins contain a C-terminal transmembrane beta-barrel and a soluble N terminus with a varying number of polypeptide-transport-associated or POTRA domains. Here we investigate Omp85 from the cyanobacterium Anabaena sp. PCC 7120. The crystallographic three-dimensional structure of the N-terminal region shows three POTRA domains, here named P1 to P3 from the N terminus. Molecular dynamics simulations revealed a hinge between P1 and P2 but in contrast show that P2 and P3 are fixed in orientation. The P2-P3 arrangement is identical as seen for the POTRA domains from proteobacterial FhaC, suggesting this orientation is a conserved feature. Furthermore, we define interfaces for protein-protein interaction in P1 and P2. P3 possesses an extended loop unique to cyanobacteria and plantae, which influences pore properties as shown by deletion. It now becomes clear how variations in structure of individual POTRA domains, as well as the different number of POTRA domains with both rigid and flexible connections make the N termini of Omp85 proteins versatile adaptors for a plentitude of functions.
bacteria, evolution, membrane proteins, protein structure, protein translocation, potra domains, membrane biogenesis
0021-9258
18016-18024
Koenig, Patrick
e03428c5-67ef-4df4-9310-77190d216517
Mirus, Oliver
2f21980b-6a60-41f3-ab68-562ae2bdff75
Haarmann, Raimund
c9200fbc-1eab-4bc9-9ab9-096cac515b74
Sommer, Maik S.
f124d403-312a-4f3a-84e9-d61e5ecba1a1
Sinning, Irmgard
fbc3f199-8a3b-47a6-9ee7-00bfc472e079
Schleiff, Enrico
119114bb-9cbb-45e9-a161-db45b1e9f4ba
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Koenig, Patrick
e03428c5-67ef-4df4-9310-77190d216517
Mirus, Oliver
2f21980b-6a60-41f3-ab68-562ae2bdff75
Haarmann, Raimund
c9200fbc-1eab-4bc9-9ab9-096cac515b74
Sommer, Maik S.
f124d403-312a-4f3a-84e9-d61e5ecba1a1
Sinning, Irmgard
fbc3f199-8a3b-47a6-9ee7-00bfc472e079
Schleiff, Enrico
119114bb-9cbb-45e9-a161-db45b1e9f4ba
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd

Koenig, Patrick, Mirus, Oliver, Haarmann, Raimund, Sommer, Maik S., Sinning, Irmgard, Schleiff, Enrico and Tews, Ivo (2010) Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85. The Journal of Biological Chemistry, 285 (23), 18016-18024. (doi:10.1074/jbc.M110.112649). (PMID:8985185)

Record type: Article

Abstract

Proteins of the Omp85 family are conserved in all kingdoms of life. They mediate protein transport across or protein insertion into membranes and reside in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. Omp85 proteins contain a C-terminal transmembrane beta-barrel and a soluble N terminus with a varying number of polypeptide-transport-associated or POTRA domains. Here we investigate Omp85 from the cyanobacterium Anabaena sp. PCC 7120. The crystallographic three-dimensional structure of the N-terminal region shows three POTRA domains, here named P1 to P3 from the N terminus. Molecular dynamics simulations revealed a hinge between P1 and P2 but in contrast show that P2 and P3 are fixed in orientation. The P2-P3 arrangement is identical as seen for the POTRA domains from proteobacterial FhaC, suggesting this orientation is a conserved feature. Furthermore, we define interfaces for protein-protein interaction in P1 and P2. P3 possesses an extended loop unique to cyanobacteria and plantae, which influences pore properties as shown by deletion. It now becomes clear how variations in structure of individual POTRA domains, as well as the different number of POTRA domains with both rigid and flexible connections make the N termini of Omp85 proteins versatile adaptors for a plentitude of functions.

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e-pub ahead of print date: 26 March 2010
Published date: 4 June 2010
Keywords: bacteria, evolution, membrane proteins, protein structure, protein translocation, potra domains, membrane biogenesis
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 200239
URI: http://eprints.soton.ac.uk/id/eprint/200239
ISSN: 0021-9258
PURE UUID: e06057d9-a4f6-4ca7-ac3e-4e4f63a6e487
ORCID for Ivo Tews: ORCID iD orcid.org/0000-0002-4704-1139

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Date deposited: 24 Oct 2011 12:23
Last modified: 17 Dec 2019 01:41

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