The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein

Lisa G. Pell, Genevieve M C Gasmi-Seabrook, Marc Morais, Philipp Neudecker, Voula Kanelis, Diane Bona, Logan W. Donaldson, Aled M. Edwards, P. Lynne Howell, Alan R. Davidson, Karen L. Maxwell

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpVC), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpVC and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpVC by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpVC structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpVC that may be important in mediating the function of this domain.

Original languageEnglish (US)
Pages (from-to)468-479
Number of pages12
JournalJournal of Molecular Biology
Volume403
Issue number3
DOIs
StatePublished - Oct 29 2010

Fingerprint

Bacteriophages
Proteins
Bacterial Structures
Immunoglobulin Domains
Computational Biology
Trypsin
Proteolysis
Immunoglobulins
Magnetic Resonance Spectroscopy
DNA

Keywords

  • Bacteriophage lambda
  • GpV
  • Ig-like domain
  • NMR structure
  • Phage tail

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Pell, L. G., Gasmi-Seabrook, G. M. C., Morais, M., Neudecker, P., Kanelis, V., Bona, D., ... Maxwell, K. L. (2010). The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein. Journal of Molecular Biology, 403(3), 468-479. https://doi.org/10.1016/j.jmb.2010.08.044

The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein. / Pell, Lisa G.; Gasmi-Seabrook, Genevieve M C; Morais, Marc; Neudecker, Philipp; Kanelis, Voula; Bona, Diane; Donaldson, Logan W.; Edwards, Aled M.; Howell, P. Lynne; Davidson, Alan R.; Maxwell, Karen L.

In: Journal of Molecular Biology, Vol. 403, No. 3, 29.10.2010, p. 468-479.

Research output: Contribution to journalArticle

Pell, LG, Gasmi-Seabrook, GMC, Morais, M, Neudecker, P, Kanelis, V, Bona, D, Donaldson, LW, Edwards, AM, Howell, PL, Davidson, AR & Maxwell, KL 2010, 'The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein', Journal of Molecular Biology, vol. 403, no. 3, pp. 468-479. https://doi.org/10.1016/j.jmb.2010.08.044
Pell, Lisa G. ; Gasmi-Seabrook, Genevieve M C ; Morais, Marc ; Neudecker, Philipp ; Kanelis, Voula ; Bona, Diane ; Donaldson, Logan W. ; Edwards, Aled M. ; Howell, P. Lynne ; Davidson, Alan R. ; Maxwell, Karen L. / The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein. In: Journal of Molecular Biology. 2010 ; Vol. 403, No. 3. pp. 468-479.
@article{d35d2056b65747888e9846366a31133a,
title = "The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein",
abstract = "Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpVC), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpVC and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpVC by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpVC structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpVC that may be important in mediating the function of this domain.",
keywords = "Bacteriophage lambda, GpV, Ig-like domain, NMR structure, Phage tail",
author = "Pell, {Lisa G.} and Gasmi-Seabrook, {Genevieve M C} and Marc Morais and Philipp Neudecker and Voula Kanelis and Diane Bona and Donaldson, {Logan W.} and Edwards, {Aled M.} and Howell, {P. Lynne} and Davidson, {Alan R.} and Maxwell, {Karen L.}",
year = "2010",
month = "10",
day = "29",
doi = "10.1016/j.jmb.2010.08.044",
language = "English (US)",
volume = "403",
pages = "468--479",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein

AU - Pell, Lisa G.

AU - Gasmi-Seabrook, Genevieve M C

AU - Morais, Marc

AU - Neudecker, Philipp

AU - Kanelis, Voula

AU - Bona, Diane

AU - Donaldson, Logan W.

AU - Edwards, Aled M.

AU - Howell, P. Lynne

AU - Davidson, Alan R.

AU - Maxwell, Karen L.

PY - 2010/10/29

Y1 - 2010/10/29

N2 - Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpVC), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpVC and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpVC by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpVC structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpVC that may be important in mediating the function of this domain.

AB - Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpVC), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpVC and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpVC by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpVC structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpVC that may be important in mediating the function of this domain.

KW - Bacteriophage lambda

KW - GpV

KW - Ig-like domain

KW - NMR structure

KW - Phage tail

UR - http://www.scopus.com/inward/record.url?scp=77957752176&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77957752176&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2010.08.044

DO - 10.1016/j.jmb.2010.08.044

M3 - Article

VL - 403

SP - 468

EP - 479

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -