3LNR
Crystal structure of poly-HAMP domains from the P. aeruginosa soluble receptor Aer2
3LNR の概要
| エントリーDOI | 10.2210/pdb3lnr/pdb |
| 分子名称 | Aerotaxis transducer Aer2, CHLORIDE ION (3 entities in total) |
| 機能のキーワード | hamp domain, poly-hamp domains, signaling protein |
| 由来する生物種 | Pseudomonas aeruginosa |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19089.73 |
| 構造登録者 | |
| 主引用文献 | Airola, M.V.,Watts, K.J.,Bilwes, A.M.,Crane, B.R. Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure, 18:436-448, 2010 Cited by PubMed Abstract: 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 three-unit poly-HAMP chain from the Pseudomonas 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 angle, 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. PubMed: 20399181DOI: 10.1016/j.str.2010.01.013 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.64 Å) |
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