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Bacteriophage lambda stabilization by auxiliary protein gpD: Timing, location, and mechanism of attachment determined by cryo-EM

Lander, Gabriel C.; Evilevitch, Alex LU ; Jeembaeva, Meerim LU ; Potter, Clinton S.; Carragher, Bridget and Johnson, John E. (2008) In Structure 16(9). p.1399-1406
Abstract
We report the cryo-EM structure of bacteriophage lambda and the mechanism for stabilizing the 20-angstrom-thick capsid containing the dsDNA genome. The crystal structure of the HK97 bacteriophage capsid fits most of the T = 7 lambda particle density with only minor adjustment. A prominent surface feature at the 3-fold axes corresponds to the cementing protein gpD, which is necessary for stabilization of the capsid shell. Its position coincides with the location of the covalent cross-link formed in the docked HK97 crystal structure, suggesting an evolutionary replacement of this gene product in lambda by autocatalytic chemistry in HK97. The crystal structure of the trimeric gpD, in which the 14 N-terminal residues required for capsid... (More)
We report the cryo-EM structure of bacteriophage lambda and the mechanism for stabilizing the 20-angstrom-thick capsid containing the dsDNA genome. The crystal structure of the HK97 bacteriophage capsid fits most of the T = 7 lambda particle density with only minor adjustment. A prominent surface feature at the 3-fold axes corresponds to the cementing protein gpD, which is necessary for stabilization of the capsid shell. Its position coincides with the location of the covalent cross-link formed in the docked HK97 crystal structure, suggesting an evolutionary replacement of this gene product in lambda by autocatalytic chemistry in HK97. The crystal structure of the trimeric gpD, in which the 14 N-terminal residues required for capsid binding are disordered, fits precisely into the corresponding EM density. The N-terminal residues of gpD are well ordered in the cryo-EM density, adding a strand to a beta-sheet formed by the capsid proteins and explaining the mechanism of particle stabilization. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Structure
volume
16
issue
9
pages
1399 - 1406
publisher
Cell Press
external identifiers
  • wos:000259164500015
  • scopus:50849118817
ISSN
0969-2126
DOI
10.1016/j.str.2008.05.016
language
English
LU publication?
yes
id
c67d74a4-92ec-46f7-b4b2-e45a38d7507d (old id 1246035)
date added to LUP
2008-11-18 14:57:26
date last changed
2017-07-23 03:39:21
@article{c67d74a4-92ec-46f7-b4b2-e45a38d7507d,
  abstract     = {We report the cryo-EM structure of bacteriophage lambda and the mechanism for stabilizing the 20-angstrom-thick capsid containing the dsDNA genome. The crystal structure of the HK97 bacteriophage capsid fits most of the T = 7 lambda particle density with only minor adjustment. A prominent surface feature at the 3-fold axes corresponds to the cementing protein gpD, which is necessary for stabilization of the capsid shell. Its position coincides with the location of the covalent cross-link formed in the docked HK97 crystal structure, suggesting an evolutionary replacement of this gene product in lambda by autocatalytic chemistry in HK97. The crystal structure of the trimeric gpD, in which the 14 N-terminal residues required for capsid binding are disordered, fits precisely into the corresponding EM density. The N-terminal residues of gpD are well ordered in the cryo-EM density, adding a strand to a beta-sheet formed by the capsid proteins and explaining the mechanism of particle stabilization.},
  author       = {Lander, Gabriel C. and Evilevitch, Alex and Jeembaeva, Meerim and Potter, Clinton S. and Carragher, Bridget and Johnson, John E.},
  issn         = {0969-2126},
  language     = {eng},
  number       = {9},
  pages        = {1399--1406},
  publisher    = {Cell Press},
  series       = {Structure},
  title        = {Bacteriophage lambda stabilization by auxiliary protein gpD: Timing, location, and mechanism of attachment determined by cryo-EM},
  url          = {http://dx.doi.org/10.1016/j.str.2008.05.016},
  volume       = {16},
  year         = {2008},
}