Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.
Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.
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DOI:
10.1016/j.str.2009.06.010
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发表时间:
2009-08-12
期刊:
影响因子:
--
通讯作者:
Sondermann H
中科院分区:
文献类型:
--
作者:
Navarro MV;De N;Bae N;Wang Q;Sondermann H
Bacterial pathogenesis involves social behavior including biofilm formation and swarming, processes that are regulated by the bacterially unique second messenger cyclic di-GMP (c-di-GMP). Diguanylate cyclases containing GGDEF and phosphodiesterases containing EAL domains have been identified as the enzymes controlling cellular c-di-GMP levels, yet less is known regarding signal transmission and the targets of c-di-GMP. FimX, a protein from Pseudomonas aeruginosa that governs twitching motility, belongs to a large subfamily containing both GGDEF and EAL domains. Biochemical and structural analyses reveals its function as a high-affinity receptor for c-di-GMP. A model for full-length FimX was generated combining solution scattering data and crystal structures of the degenerate GGDEF and EAL domains. While FimX forms a dimer in solution via the N-terminal domains, a crystallographic EAL domain dimer suggests modes for the regulation of FimX by c-di-GMP binding. The results provide the structural basis for c-di-GMP sensing via degenerate phosphodiesterases.
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DOI:
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发表时间:
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影响因子:
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通讯作者:
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DOI:
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发表时间:
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期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
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通讯作者:
Kleywegt, GJ