Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis.
Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis.
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DOI:
10.1016/j.str.2012.04.011
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发表时间:
2012-07-03
期刊:
影响因子:
5.7
通讯作者:
Buchanan, Susan K.
中科院分区:
文献类型:
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作者:
Fairman, James W.;Dautin, Nathalie;Wojtowicz, Damian;Liu, Wei;Noinaj, Nicholas;Barnard, Travis J.;Udho, Eshwar;Przytycka, Teresa M.;Cherezov, Vadim;Buchanan, Susan K.
Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They contain C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal β-domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin β-domain and use this information to solve its structure and the β-domain structure of a Y. pseudotuberculosis invasin. Both β-domain structures crystallized as monomers and reveal that the previous range of residues assigned to the β-domain also includes a protease resistant domain that is part of the passenger. Additionally, we identify 146 non-redundant representative members of the intimin/invasin family based on the boundaries of the highly conserved intimin and invasin β-domains. We then use this set of sequences along with our structural data to find and map the evolutionarily constrained residues within the β-domain.
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
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通讯作者:
Cowtan, K
影响因子:
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作者:
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通讯作者:
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