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Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.

Meng G, St Geme JW, Waksman G - J. Mol. Biol. (2008)

Bottom Line: Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function.Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters.Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.

View Article: PubMed Central - PubMed

Affiliation: Institute of Structural and Molecular Biology at UCL/Birkbeck, London, UK.

ABSTRACT
The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adherence to the respiratory epithelium. In this report, we show that the structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains. Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function. Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters. Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.

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The repetitive domain arrangement of nonencapsulated H. influenzae Hia and encapsulated H. influenzae Hsf. The sequences in Hia that are determined crystallographically in this report are highlighted with purple brackets.
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fig1: The repetitive domain arrangement of nonencapsulated H. influenzae Hia and encapsulated H. influenzae Hsf. The sequences in Hia that are determined crystallographically in this report are highlighted with purple brackets.

Mentions: To gain insight into the structure of the full-length Hia protein, the Hia amino acid sequence was submitted to the daTAA server,† a server designed to analyze sequences of trimeric autotransporters.19 As shown in Fig. 1, the sequence analysis predicted an impressive multirepetitive domain arrangement (Fig. 1) consisting of five domain types, with some repeated several times along the sequence. The Hia sequence contains five so-called “Trp-ring” domains (residues 117–166, 263–319, 372–421, 481–530, and 654–705, designated W1, W2, W3, W4, and W5, respectively, in Fig. 1) and three so-called “Neck” domains, including two domains with functional insertions (referred to as “IsNeck” domains; residues 53–113, 589–650, and 975–996, designated IN1, IN2, and Neck, respectively, in Fig. 1). In addition, there are two so-called “KG” domains (residues 320–372 and 743–798, designated KG1 and KG2, respectively, in Fig. 1), one so-called “GANG” domain (residues 180–263), one so-called “TTT” domain (residues 842–974), one signal peptide (residues 1–49, designated SP in Fig. 1), and one membrane anchor/translocator domain (residues 1022–1098, designated “TM” in Fig. 1). The distinctive features of the Trp-ring, Neck, IsNeck, KG, GANG, and TTT domains are well described‡.19


Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter.

Meng G, St Geme JW, Waksman G - J. Mol. Biol. (2008)

The repetitive domain arrangement of nonencapsulated H. influenzae Hia and encapsulated H. influenzae Hsf. The sequences in Hia that are determined crystallographically in this report are highlighted with purple brackets.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2597055&req=5

fig1: The repetitive domain arrangement of nonencapsulated H. influenzae Hia and encapsulated H. influenzae Hsf. The sequences in Hia that are determined crystallographically in this report are highlighted with purple brackets.
Mentions: To gain insight into the structure of the full-length Hia protein, the Hia amino acid sequence was submitted to the daTAA server,† a server designed to analyze sequences of trimeric autotransporters.19 As shown in Fig. 1, the sequence analysis predicted an impressive multirepetitive domain arrangement (Fig. 1) consisting of five domain types, with some repeated several times along the sequence. The Hia sequence contains five so-called “Trp-ring” domains (residues 117–166, 263–319, 372–421, 481–530, and 654–705, designated W1, W2, W3, W4, and W5, respectively, in Fig. 1) and three so-called “Neck” domains, including two domains with functional insertions (referred to as “IsNeck” domains; residues 53–113, 589–650, and 975–996, designated IN1, IN2, and Neck, respectively, in Fig. 1). In addition, there are two so-called “KG” domains (residues 320–372 and 743–798, designated KG1 and KG2, respectively, in Fig. 1), one so-called “GANG” domain (residues 180–263), one so-called “TTT” domain (residues 842–974), one signal peptide (residues 1–49, designated SP in Fig. 1), and one membrane anchor/translocator domain (residues 1022–1098, designated “TM” in Fig. 1). The distinctive features of the Trp-ring, Neck, IsNeck, KG, GANG, and TTT domains are well described‡.19

Bottom Line: Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function.Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters.Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.

View Article: PubMed Central - PubMed

Affiliation: Institute of Structural and Molecular Biology at UCL/Birkbeck, London, UK.

ABSTRACT
The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adherence to the respiratory epithelium. In this report, we show that the structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains. Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function. Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters. Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.

Show MeSH
Related in: MedlinePlus