IPR022796
Chlorophyll A-B binding protein
InterPro entry
Short name | Chloroa_b-bind |
family relationships |
Description
The light-harvesting complex (LHC) consists of chlorophylls A and B and the chlorophyll A-B binding protein. LHC functions as a light receptor that captures and delivers excitation energy to photosystems I and II with which it is closely associated. Under changing light conditions, the reversible phosphorylation of light harvesting chlorophyll a/b binding proteins (LHCII) represents a system for balancing the excitation energy between the two photosystems
[1].
The N terminus of the chlorophyll A-B binding protein extends into the stroma where it is involved with adhesion of granal membranes and photo-regulated by reversible phosphorylation of its threonine residues
[3]. Both these processes are believed to mediate the distribution of excitation energy between photosystems I and II.
This family also includes the photosystem II protein PsbS, which plays a role in energy-dependent quenching that increases thermal dissipation of excess absorbed light energy in the photosystem
[2].
References
1.NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina. Liu XD, Shen YG. FEBS Lett. 569, 337-40, (2004). View articlePMID: 15225658
2.Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein. Li XP, Gilmore AM, Caffarri S, Bassi R, Golan T, Kramer D, Niyogi KK. J. Biol. Chem. 279, 22866-74, (2004). View articlePMID: 15033974
3.The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis. Yang DH, Paulsen H, Andersson B. FEBS Lett. 466, 385-8, (2000). View articlePMID: 10682866
Contributing Member Database Entry
- Pfam:PF00504
Representative structure
6a2w: Crystal structure of fucoxanthin chlorophyll a/c complex from Phaeodactylum tricornutum