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Structure of serine acetyltransferase from Haemophilus influenzae Rd.

Gorman J, Shapiro L
Acta Crystallogr D Biol Crystallogr 60 1600-5 (2004)
Cited: 20 times
EuropePMC logo PMID: 15333931

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.

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Reviews citing this publication (3)

  1. Functional analysis of the cysteine synthase protein complex from plants: structural, biochemical and regulatory properties. Wirtz M, Hell R. J Plant Physiol 163 273-286 (2006)
  2. The cysteine regulatory complex from plants and microbes: what was old is new again. Jez JM, Dey S. Curr Opin Struct Biol 23 302-310 (2013)
  3. Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens. Hicks JL, Oldham KEA, McGarvie J, Walker EJ. Biosci Rep 42 BSR20220368 (2022)

Articles citing this publication (15)

  1. Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex. Francois JA, Kumaran S, Jez JM. Plant Cell 18 3647-3655 (2006)
  2. Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A. Protein Sci 14 2115-2124 (2005)
  3. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. Huang B, Vetting MW, Roderick SL. J Bacteriol 187 3201-3205 (2005)
  4. A mechanistic model of the cysteine synthase complex. Feldman-Salit A, Wirtz M, Hell R, Wade RC. J Mol Biol 386 37-59 (2009)
  5. Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, Bettati S, Dodatko T, Cozzini P, Kellogg GE, Cook PF, Roderick SL, Mozzarelli A. J Med Chem 53 345-356 (2010)
  6. Fusel alcohols regulate translation initiation by inhibiting eIF2B to reduce ternary complex in a mechanism that may involve altering the integrity and dynamics of the eIF2B body. Taylor EJ, Campbell SG, Griffiths CD, Reid PJ, Slaven JW, Harrison RJ, Sims PF, Pavitt GD, Delneri D, Ashe MP. Mol Biol Cell 21 2202-2216 (2010)
  7. Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form a cysteine synthase complex. Kumar S, Raj I, Nagpal I, Subbarao N, Gourinath S. J Biol Chem 286 12533-12541 (2011)
  8. A two-step process controls the formation of the bienzyme cysteine synthase complex. Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, Cook PF, Mozzarelli A. J Biol Chem 285 12813-12822 (2010)
  9. Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone. Yi H, Dey S, Kumaran S, Lee SG, Krishnan HB, Jez JM. J Biol Chem 288 36463-36472 (2013)
  10. Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex. Benoni R, De Bei O, Paredi G, Hayes CS, Franko N, Mozzarelli A, Bettati S, Campanini B. FEBS Lett 591 1212-1224 (2017)
  11. Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Guan R, Roderick SL, Huang B, Cook PF. Biochemistry 47 6322-6328 (2008)
  12. Crystal structure of serine acetyl transferase from Brucella abortus and its complex with coenzyme A. Kumar S, Kumar N, Alam N, Gourinath S. Biochim Biophys Acta 1844 1741-1748 (2014)
  13. Interaction between cysteine synthase and serine O-acetyltransferase proteins and their stage specific expression in Leishmania donovani. Singh K, Singh KP, Equbal A, Suman SS, Zaidi A, Garg G, Pandey K, Das P, Ali V. Biochimie 131 29-44 (2016)
  14. Bioinformatics analysis of enzymes involved in cysteine biosynthesis: first evidence for the formation of cysteine synthase complex in cyanobacteria. Kharwar S, Bhattacharjee S, Mishra AK. 3 Biotech 11 354 (2021)
  15. Recombinant production of active Streptococcus pneumoniae CysE in E. coli facilitated by codon optimized BL21(DE3)-RIL and detergent. Verma D, Antil M, Gupta V. Prep Biochem Biotechnol 49 368-374 (2019)


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