Prediction of structure and organisation of chlorophyll a/b binding polypeptides in PS I and II.
Indian J Biochem Biophys
;
1997 Aug; 34(4): 341-6
Artículo
en Inglés
| IMSEAR
| ID: sea-26435
ABSTRACT
Secondary structures, functionally important residues, antigenic sites, membrane spanning segments and hydropathicity of light harvesting chlorophyll a/b binding polypeptides (LHC) are predicted by theoretical methods from the amino acid sequence of the polypeptides. The reported structural features of the Pea LHC (Lhcb 1 gene product) from electron crystallographic studies have been compared by alignment with other types of chlorophyll a/b binding polypeptides for structural prediction. Fifteen conserved residues D85, D89, E113, H116, E/Q133, E/Q181, E189, D/N233, E252, N/H255, Q/E269, E/D/Q280, N281, H285, D288 (number indicates position in the aligned sequence), are identified which are potential ligands to Mg2+ of chlorophylls. Three amino acid residues D89, E/Q131 and D/N 233 are proposed as ligands to chlorophylls b2, a7 and b2 respectively, for which ligands are not identified in electron crystallographic study.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Sitios de Unión
/
Datos de Secuencia Molecular
/
Clorofila
/
Secuencia de Aminoácidos
/
Homología de Secuencia de Aminoácido
/
Estructura Secundaria de Proteína
/
Proteínas del Complejo del Centro de Reacción Fotosintética
/
Complejos de Proteína Captadores de Luz
Tipo de estudio:
Estudio pronóstico
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1997
Tipo del documento:
Artículo
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