1s80

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spinqualitylabelsall models 1s80, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Serine Acetyltranferase from Haemophilis influenzae Rd

Overview

The crystal structure of serine acetyltransferase (SAT) from Haemophilus influenzae Rd determined at 2.7 A resolution is presented. SAT is a member of a family of hexapeptide-containing transferases that contain six-residue tandem repeats (LIV)-G-X(4) that have been shown to form left-handed parallel beta-helices. In the current structure, each protomer is comprised of two domains: an N-terminal alpha-helical domain and a C-terminal left-handed parallel beta-helix domain. Although other members of this protein family are known to form trimeric structures, SAT forms a dimer of trimers in which the trimer interface is mediated through interactions between both the beta-helix domains and N-terminal domains; these trimers dimerize through contacts in the N-terminal domain. All dimer-of-trimer interactions are mediated through amino acids within an N-terminal extension common only to a subset of SATs, suggesting that members of this subfamily may also adopt hexameric structures. Putative active sites are formed by crevices between adjacent protomers in a trimer. Thus, six independent active sites exist in the hexameric enzyme complex.

About this Structure

1S80 is a Single protein structure of sequence from Haemophilus influenzae. Active as Serine O-acetyltransferase, with EC number 2.3.1.30 Full crystallographic information is available from OCA.

Reference

Structure of serine acetyltransferase from Haemophilus influenzae Rd., Gorman J, Shapiro L, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1600-5. Epub 2004, Aug 26. PMID:15333931

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