1s80

Structure of Serine Acetyltransferase from Haemophilis influenzae Rd

spinqualitylabelsall models 1s80, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1s80 is a 6 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: CYSE, HI0606 (Haemophilus influenzae) Activity: Serine O-acetyltransferase, with EC number 2.3.1.30 Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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