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1smd
From Proteopedia
| 1smd, resolution 1.60Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||||
| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
HUMAN SALIVARY AMYLASE
Salivary alpha-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 (beta/alpha)(8-) barrel structure, domain B has no definite topology and domain C has a Greek-key barrel structure. The Ca(2+) ion is bound to Asnl00, 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.
Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. PMID:15299664
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1SMD is a 1 chain structure with sequence from Homo sapiens. The February 2006 RCSB PDB Molecule of the Month feature on Alpha-amylase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_2. Full crystallographic information is available from OCA.
Reference
- Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ. Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. PMID:15299664 doi:10.1107/S0907444995014119
Page seeded by OCA on Thu Jan 21 09:25:22 2010
