A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-06

AUTHORS

Florante A. Quiocho, Meenakshi N. Vyas, Nand K. Vyas

ABSTRACT

The refined 1.9-A resolution structure of the periplasmic D-galactose-binding protein (GBP) reveals a calcium ion surrounded by seven ligands, all protein oxygen atoms. A nine-residue loop (amino-acid positions 134-142), which is preceded by a beta-turn and followed by a beta-strand, provides five ligands from every second residue. The last two ligands are supplied by the carboxylate group of Glu 205. The entire GBP Ca2+-binding site adopts a conformation very similar to the site in the 'helix-loop-helix' or 'EF-hand' unit commonly found in intracellular calcium-binding proteins, but without the two helices. Structural analyses have also uncovered the sugar-binding site some 30 A from the calcium and a site for interacting with the membrane-bound trg chemotactic signal transducer approximately 45 A from the calcium. Our results show that a common tight calcium binding site of ancient origin can be tethered to different secondary structures. They also provide the first demonstration of a metal-binding site in a protein which is involved in bacterial active transport and chemotaxis. More... »

PAGES

635

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/327635a0

DOI

http://dx.doi.org/10.1038/327635a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049210651

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3600760


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