Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimer.
Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimer.
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DOI:
10.1126/science.1202997
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发表时间:
2011-06-03
期刊:
影响因子:
--
通讯作者:
Hochstrasser RM
中科院分区:
文献类型:
--
作者:
Remorino A;Korendovych IV;Wu Y;DeGrado WF;Hochstrasser RM
Two dimensional vibrational echo spectroscopy has previously been applied to structural determination of small peptides. Here we extend the technique to a more complex, biologically significant system: the homodimeric transmembrane dimer from the α-chain of the integrin αIIbβ3. We prepared micelle suspensions of the pair of 30-residue chains that span the membrane in the native structure, with varying levels of heavy (13C=18O) isotopes substituted in the backbone of the central 10th through 20th positions. The constraints derived from vibrational coupling of the precisely spaced heavy residues led to determination of an optimized structure from a range of model candidates: Glycine residues at the 12th, 15th and 16th positions form a tertiary contact in parallel right handed helix dimers with crossing angles of −58° ± 9° and interhelical distances of 7.7 ± 0.5 Å. The frequency correlation established the dynamical model used in the analysis and it indicated the absence of mobile water associated with labeled residues. Delocalization of vibrational excitations between the helices was also quantitatively established.
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