Structure of human salivary α-amylase at 1.6 Å resolution: Implications for its role in the oral cavity

Narayanan Ramasubbu, Venugopalan Paloth, Yaoguang Luo, Gary D. Brayer, Michael J. Levine

Research output: Contribution to journalArticlepeer-review

197 Scopus citations

Abstract

Salivary α-amylase, a major component of human saliva, plays a role in the initial digestion of starch and may be involved in the colonization of bacteria involved in early dental plaque formation. The three-dimensional atomic structure of salivary amylase has been determined to understand the structure-function relationships of this enzyme. This structure was refined to an R value of 18.4% with 496 amino-acid residues, one calcium ion, one chloride ion and 170 water molecules. Salivary amylase folds into a multidomain structure consisting of three domains, A, B and C. Domain A has a (β/α)8-barrel structure, domain B has no definite topology and domain C has a Greek-key barrel structure. The Ca2+ ion is bound to Asn100, Arg158, Asp167, His201 and three water molecules. The Cl- ion is bound to Arg195, Asn298 and Arg337 and one water molecule. The highly mobile glycine-rich loop 304-310 may act as a gateway for substrate binding and be involved in a 'trap-release' mechanism in the hydrolysis of substrates. Strategic placement of calcium and chloride ions, as well as histidine and tryptophan residues may play a role in differentiating between the glycone and aglycone ends of the polysaccharide substrates. Salivary amylase also possesses a suitable site for binding to enamel surfaces and provides potential sites for the binding of bacterial adhesins.

Original languageEnglish (US)
Pages (from-to)435-446
Number of pages12
JournalActa Crystallographica Section D: Biological Crystallography
Volume52
Issue number3
DOIs
StatePublished - May 1 1996
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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