Novel tertiary structures and stereospecificities of periplasmic binding proteins involved in active transport and chemotaxis.
J Biosci
;
1985 Aug; 8(1&2): 461-470
Artículo
en Inglés
| IMSEAR
| ID: sea-160413
ABSTRACT
Binding proteins, which are located in the periplasmic space of Gram-negative bacteria, are essential components of osmotic shock-sensitive active transport systems and Chemotaxis. Described briefly herein are the high resolution molecular structures of four binding proteins specific for (i) L-arabinose, (ii) sulphate, (iii) D-galactose, and (iv) leucine, isoleucine or valine which we have recently determined. The first three proteins contained bound substrates. Several novel substrate binding properties of the arabinose- and sulphatebinding proteins as revealed by structure refinement at 1·7 Å resolution are also presented. These results have profound significance in understanding both protein structures and substrate-protein interactions.
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IMSEAR (Asia Sudoriental)
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Inglés
Revista:
J Biosci
Año:
1985
Tipo del documento:
Artículo
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