1S80

Structure of Serine Acetyltransferase from Haemophilis influenzae Rd

Summary for 1S80

• Entry DOI: 10.2210/pdb1s80/pdb
• Descriptor: Serine acetyltransferase (2 entities in total)
• Functional Keywords: structural genomics; protein structure initiative; serine acetyltransferase; left-handed parallel beta-helix; nysgxrc, psi, new york sgx research center for structural genomics, nysgxrc, transferase
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 6
• Total formula weight: 183793.27

Authors

Gorman, J.,Gogos, A.,Shapiro, L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2004-01-30, release date: 2004-08-31, Last modification date: 2024-10-30)

Primary citation

Gorman, J.,Shapiro, L.
Structure of serine acetyltransferase from Haemophilus influenzae Rd.
Acta Crystallogr.,Sect.D, 60:1600-1605, 2004

PubMed Abstract: 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.

PubMed: 15333931
DOI: 10.1107/S0907444904015240

Experimental method

X-RAY DIFFRACTION (2.7 Å)