Structure of concatenated HAMP domains provides a mechanism for signal transduction.
Structure of concatenated HAMP domains provides a mechanism for signal transduction.
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DOI:
10.1016/j.str.2010.01.013
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发表时间:
2010-03-14
期刊:
影响因子:
--
通讯作者:
Crane BR
中科院分区:
文献类型:
--
作者:
Airola MV;Watts KJ;Bilwes AM;Crane BR
HAMP domains are widespread prokaryotic signaling modules found as single domains or poly-HAMP chains in both transmembrane and soluble proteins. The crystal structure of a 3 unit poly-HAMP chain from the P. aeruginosa soluble receptor Aer2 defines a universal parallel four-helix bundle architecture for diverse HAMP domains. Two contiguous domains integrate to form a concatenated di-HAMP structure. The three HAMP domains display two distinct conformations that differ by changes in helical register, crossing angles, and rotation. These conformations are stabilized by different subsets of conserved residues. Known signals delivered to HAMP would be expected to switch the relative stability of the two conformations and the position of a coiled-coil phase stutter at the junction with downstream helices. We propose that the two conformations represent opposing HAMP signaling states and suggest a signaling mechanism whereby HAMP domains interconvert between the two states, which alternate down a poly-HAMP chain.
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影响因子:
2.9
作者:
Draheim, RR;Bormans, AF;Manson, MD
通讯作者:
Manson, MD
影响因子:
2.1
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:
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作者:
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通讯作者:
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