Structure of the membrane protein FhaC:: A member of the Omp85-TpsB transporter superfamily

被引:209
作者
Clantin, Bernard
Delattre, Anne-Sophie
Rucktooa, Prakash
Saint, Nathalie
Meli, Albano C.
Locht, Camille
Jacob-Dubuisson, Francoise
Villeret, Vincent
机构
[1] Univ Lille 2, UMR8161, CNRS, Inst Biol Lille, F-59021 Lille, France
[2] Inst Pasteur, F-59019 Lille, France
[3] IFR142, F-59019 Lille, France
[4] INSERM, U629, F-59019 Lille, France
[5] INSERM, U629, F-34090 Montpellier, France
[6] INSERM, U554, F-34090 Montpellier, France
[7] Univ Montpellier 1, CNRS, UMR5048, Montpellier, France
[8] Univ Montpellier 2, Montpellier, France
关键词
D O I
10.1126/science.1143860
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
In Gram-negative bacteria and eukaryotic organelles, beta-barrel proteins of the outer membrane protein 85-two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 angstrom crystal structure of FhaC. The transporter comprises a 16-stranded beta barrel that is occluded by an N-terminal alpha helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport-associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.
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页码:957 / 961
页数:5
相关论文
共 25 条
[1]   Origin of a chloroplast protein importer [J].
Bölter, B ;
Soll, J ;
Schulz, A ;
Hinnah, S ;
Wagner, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (26) :15831-15836
[2]   The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway [J].
Clantin, B ;
Hodak, H ;
Willery, E ;
Locht, C ;
Jacob-Dubuisson, F ;
Villeret, V .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (16) :6194-6199
[3]  
DeLano W.L, 2002, The Pymol Molecular Graphics System Version 1.0
[4]   The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria [J].
Gentle, I ;
Gabriel, K ;
Beech, P ;
Waller, R ;
Lithgow, T .
JOURNAL OF CELL BIOLOGY, 2004, 164 (01) :19-24
[5]   Molecular architecture and function of the Omp85 family of proteins [J].
Gentle, IE ;
Burri, L ;
Lithgow, T .
MOLECULAR MICROBIOLOGY, 2005, 58 (05) :1216-1225
[6]   Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin [J].
Guédin, S ;
Willery, E ;
Tommassen, J ;
Fort, E ;
Drobecq, H ;
Locht, C ;
Jacob-Dubuisson, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (39) :30202-30210
[7]   Reconstitution of a chloroplast protein import channel [J].
Hinnah, SC ;
Hill, K ;
Wagner, R ;
Schlicher, T ;
Soll, J .
EMBO JOURNAL, 1997, 16 (24) :7351-7360
[8]   Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate [J].
Hodak, Helene ;
Clantin, Bernard ;
Willery, Eve ;
Villeret, Vincent ;
Locht, Camille ;
Jacob-Dubuisson, Francoise .
MOLECULAR MICROBIOLOGY, 2006, 61 (02) :368-382
[9]   Protein secretion through autotransporter and two-partner pathways [J].
Jacob-Dubuisson, F ;
Fernandez, R ;
Coutte, L .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2004, 1694 (1-3) :235-257
[10]   Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins [J].
Kajava, AV ;
Cheng, N ;
Cleaver, R ;
Kessel, M ;
Simon, MN ;
Willery, E ;
Jacob-Dubuisson, F ;
Locht, C ;
Steven, AC .
MOLECULAR MICROBIOLOGY, 2001, 42 (02) :279-292