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Transferase PDB id
1sst
Jmol
Contents
Protein chains
233 a.a. *
Ligands
COA ×3
Waters ×172
* Residue conservation analysis
PDB id:
1sst
Name: Transferase
Title: Serine acetyltransferase- complex with coa
Structure: Serine acetyltransferase. Chain: a, b, c. Synonym: sat. Engineered: yes
Source: Haemophilus influenzae. Organism_taxid: 727. Gene: cyse, hi0606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Hexamer (from PDB file)
Resolution:
2.00Å     R-factor:   0.223     R-free:   0.270
Authors: L.R.Olsen,B.Huang,M.W.Vetting,S.L.Roderick
Key ref:
L.R.Olsen et al. (2004). Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor. Biochemistry, 43, 6013-6019. PubMed id: 15147185 DOI: 10.1021/bi0358521
Date:
24-Mar-04     Release date:   01-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P43886  (CYSE_HAEIN) -  Serine acetyltransferase
Seq:
Struc: 		267 a.a.
233 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.30  - Serine O-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Acetyl-CoA
 + L-serine
 =
CoA
Bound ligand (Het Group name = COA)
corresponds exactly 		+ O-acetyl-L-serine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cellular amino acid biosynthetic process   3 terms 
  Biochemical function     transferase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi0358521 Biochemistry 43:6013-6019 (2004)
PubMed id: 15147185  
 
 
Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor.
L.R.Olsen, B.Huang, M.W.Vetting, S.L.Roderick.
 
  ABSTRACT  
 
Serine acetyltransferase (SAT, EC 2.3.1.30) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of l-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of l-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. We have determined the X-ray crystal structure of Haemophilus influenzae SAT in complexes with CoA and its cysteine feedback inhibitor. The enzyme is a 175 kDa hexamer displaying the characteristic left-handed parallel beta-helix (LbetaH) structural domain of the hexapeptide acyltransferase superfamily of enzymes. Cysteine is bound in a crevice between adjacent LbetaH domains and underneath a loop excluded from the coiled LbetaH. The proximity of its thiol group to the thiol group of CoA derived from superimposed models of the cysteine and CoA complexes confirms that cysteine is bound at the active site. Analysis of the contacts of SAT with cysteine and CoA and the conformational differences that distinguish these complexes provides a structural basis for cysteine feedback inhibition, which invokes competition between cysteine and serine binding and a cysteine-induced conformational change of the C-terminal segment of the enzyme that excludes binding of the cofactor.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19928859 E.Salsi, A.S.Bayden, F.Spyrakis, A.Amadasi, B.Campanini, S.Bettati, T.Dodatko, P.Cozzini, G.E.Kellogg, P.F.Cook, S.L.Roderick, and A.Mozzarelli (2010).
Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature.
  J Med Chem, 53, 345-356.
PDB codes: 3iqg 3iqh 3iqi
20364282 H.Yi, G.E.Ravilious, A.Galant, H.B.Krishnan, and J.M.Jez (2010).
From sulfur to homoglutathione: thiol metabolism in soybean.
  Amino Acids, 39, 963-978.  
19213732 S.Kumaran, H.Yi, H.B.Krishnan, and J.M.Jez (2009).
Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions.
  J Biol Chem, 284, 10268-10275.  
  19098440 K.C.Kunes, S.C.Clark, D.L.Cox, and R.R.Singh (2008).
Left handed beta helix models for mammalian prion fibrils.
  Prion, 2, 81-90.  
18498176 R.Guan, S.L.Roderick, B.Huang, and P.F.Cook (2008).
Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae.
  Biochemistry, 47, 6322-6328.  
17519228 A.K.Bergfeld, H.Claus, U.Vogel, and M.Mühlenhoff (2007).
Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1.
  J Biol Chem, 282, 22217-22227.  
17644602 R.Pinto, J.S.Harrison, T.Hsu, W.R.Jacobs, and T.S.Leyh (2007).
Sulfite reduction in mycobacteria.
  J Bacteriol, 189, 6714-6722.  
16854983 F.Liu, B.C.Yoo, J.Y.Lee, W.Pan, and A.C.Harmon (2006).
Calcium-regulated phosphorylation of soybean serine acetyltransferase in response to oxidative stress.
  J Biol Chem, 281, 27405-27415.  
16386330 M.Wirtz, and R.Hell (2006).
Functional analysis of the cysteine synthase protein complex from plants: structural, biochemical and regulatory properties.
  J Plant Physiol, 163, 273-286.  
15948956 A.Müller, G.H.Thomas, R.Horler, J.A.Brannigan, E.Blagova, V.M.Levdikov, M.J.Fogg, K.S.Wilson, and A.J.Wilkinson (2005).
An ATP-binding cassette-type cysteine transporter in Campylobacter jejuni inferred from the structure of an extracytoplasmic solute receptor protein.
  Mol Microbiol, 57, 143-155.
PDB code: 1xt8
15987896 B.Campanini, F.Speroni, E.Salsi, P.F.Cook, S.L.Roderick, B.Huang, S.Bettati, and A.Mozzarelli (2005).
Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy.
  Protein Sci, 14, 2115-2124.  
15838047 B.Huang, M.W.Vetting, and S.L.Roderick (2005).
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.
  J Bacteriol, 187, 3201-3205.
PDB code: 1y7l
15901700 B.Sperandio, P.Polard, D.S.Ehrlich, P.Renault, and E.Guédon (2005).
Sulfur amino acid metabolism and its control in Lactococcus lactis IL1403.
  J Bacteriol, 187, 3762-3778.  
16307301 M.Wirtz, and M.Droux (2005).
Synthesis of the sulfur amino acids: cysteine and methionine.
  Photosynth Res, 86, 345-362.  
16307305 T.G.Sors, D.R.Ellis, and D.E.Salt (2005).
Selenium uptake, translocation, assimilation and metabolic fate in plants.
  Photosynth Res, 86, 373-389.  
15941393 T.G.Sors, D.R.Ellis, G.N.Na, B.Lahner, S.Lee, T.Leustek, I.J.Pickering, and D.E.Salt (2005).
Analysis of sulfur and selenium assimilation in Astragalus plants with varying capacities to accumulate selenium.
  Plant J, 42, 785-797.  
15231846 V.E.Pye, A.P.Tingey, R.L.Robson, and P.C.Moody (2004).
The structure and mechanism of serine acetyltransferase from Escherichia coli.
  J Biol Chem, 279, 40729-40736.
PDB code: 1t3d
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.