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Exploring the structure of the 100 amino-acid residue long N-terminus of the plant antenna protein CP29.

Abstract：

:The structure of the unusually long (∼100 amino-acid residues) N-terminal domain of the light-harvesting protein CP29 of plants is not defined in the crystal structure of this membrane protein. We studied the N-terminus using two electron paramagnetic resonance (EPR) approaches: the rotational diffusion of spin labels at 55 residues with continuous-wave EPR, and three sets of distances with a pulsed EPR method. The N-terminus is relatively structured. Five regions that differ considerably in their dynamics are identified. Two regions have low rotational diffusion, one of which shows α-helical character suggesting contact with the protein surface. This immobile part is flanked by two highly dynamic, unstructured regions (loops) that cover residues 10-22 and 82-91. These loops may be important for the interaction with other light-harvesting proteins. The region around residue 4 also has low rotational diffusion, presumably because it attaches noncovalently to the protein. This section is close to a phosphorylation site (Thr-6) in related proteins, such as those encoded by the Lhcb4.2 gene. Phosphorylation might influence the interaction with other antenna complexes, thereby regulating the supramolecular organization in the thylakoid membrane.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Shabestari MH,Wolfs CJ,Spruijt RB,van Amerongen H,Huber M

doi

10.1016/j.bpj.2013.11.4506

subject

Has Abstract

pub_date

2014-03-18 00:00:00

pages

1349-58

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(14)00131-3

journal_volume

106

pub_type

杂志文章

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