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PDBsum entry 1kru

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1kru
Jmol
Contents
Protein chains
201 a.a. *
Ligands
COA ×3
IPT ×6
Waters ×95
* Residue conservation analysis
PDB id:
1kru
Name: Transferase
Title: Galactoside acetyltransferase in complex with iptg and coenzyme a
Structure: Galactoside o-acetyltransferase. Chain: a, b, c. Synonym: thiogalactoside acetyltransferase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: laca. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PQS)
Resolution:
2.80Å     R-factor:   0.172     R-free:   0.247
Authors: X.-G.Wang,L.R.Olsen,S.L.Roderick
Key ref:
X.G.Wang et al. (2002). Structure of the lac operon galactoside acetyltransferase. Structure, 10, 581-588. PubMed id: 11937062 DOI: 10.1016/S0969-2126(02)00741-4
Date:
10-Jan-02     Release date:   10-Apr-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07464  (THGA_ECOLI) -  Galactoside O-acetyltransferase
Seq:
Struc:
203 a.a.
201 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.18  - Galactoside O-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
Acetyl-CoA
Bound ligand (Het Group name = COA)
matches with 94.00% similarity
+
beta-D-galactoside
Bound ligand (Het Group name = IPT)
matches with 64.00% similarity
= CoA
+ 6-acetyl-beta-D-galactoside
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     lactose biosynthetic process   1 term 
  Biochemical function     transferase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0969-2126(02)00741-4 Structure 10:581-588 (2002)
PubMed id: 11937062  
 
 
Structure of the lac operon galactoside acetyltransferase.
X.G.Wang, L.R.Olsen, S.L.Roderick.
 
  ABSTRACT  
 
The galactoside acetyltransferase (thiogalactoside transacetylase) of Escherichia coli (GAT, LacA, EC 2.3.1.18) is a gene product of the classical lac operon. GAT may assist cellular detoxification by acetylating nonmetabolizable pyranosides, thereby preventing their reentry into the cell. The structure of GAT has been solved in binary complexes with acetyl-CoA or CoA and in ternary complexes with CoA and the nonphysiological acceptor substrates isopropyl beta-D-thiogalactoside (IPTG) or p-nitrophenyl beta-D-galactopyranoside (PNPbetaGal). A hydrophobic cleft that binds the thioisopropyl and p-nitrophenyl aglycones of IPTG and PNPbetaGal may discriminate against substrates with hydrophilic substituents at this position, such as lactose, or inducers of the lac operon. An extended loop projecting from the left-handed parallel beta helix domain contributes His115, which is in position to facilitate attack of the C6-hydroxyl group of the substrate on the thioester.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Comparison of the Active Sites of GAT and PaXAT(A) Stereo diagrams of the GAT acetyl-CoA complex with IPTG molecules from the GAT IPTG/CoA complex superimposed. A line segment joins the C6-hydroxyl group of the proximal IPTG and the acetyl carbonyl carbon atom of acetyl-CoA (distance 1.7 Å).(B) The PaXAT chloramphenicol/desulpho-CoA complex viewed perpendicular to the molecular 3-fold axis. The view is similar to GAT depicted in Figure 1B and shows the ligands present at just one active site for clarity.(C) The active site of the PaXAT chloramphenicol/desulpho-CoA complex (desulpho-CoA not shown).(D) Stereo diagram of the active site of the PaXAT chloramphenicol/desulpho-CoA complex.
 
  The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 581-588) copyright 2002.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19655786 C.M.Bartling, and C.R.Raetz (2009).
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.
  Biochemistry, 48, 8672-8683.
PDB code: 3eh0
19525232 H.J.Lee, B.Rakić, M.Gilbert, W.W.Wakarchuk, S.G.Withers, and N.C.Strynadka (2009).
Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.
  J Biol Chem, 284, 24501-24511.
PDB codes: 2wlc 2wld 2wle 2wlf 2wlg
18422345 C.M.Bartling, and C.R.Raetz (2008).
Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
  Biochemistry, 47, 5290-5302.  
18667421 N.B.Olivier, and B.Imperiali (2008).
Crystal Structure and Catalytic Mechanism of PglD from Campylobacter jejuni.
  J Biol Chem, 283, 27937-27946.
PDB codes: 3bss 3bsw 3bsy
18408022 N.Jimenez, R.Canals, M.T.Saló, S.Vilches, S.Merino, and J.M.Tomás (2008).
The Aeromonas hydrophila wb*O34 gene cluster: genetics and temperature regulation.
  J Bacteriol, 190, 4198-4209.  
17650509 A.Faye, C.Esnous, N.T.Price, M.A.Onfray, J.Girard, and C.Prip-Buus (2007).
Rat liver carnitine palmitoyltransferase 1 forms an oligomeric complex within the outer mitochondrial membrane.
  J Biol Chem, 282, 26908-26916.  
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.  
17991990 T.Kalisky, E.Dekel, and U.Alon (2007).
Cost-benefit theory and optimal design of gene regulation functions.
  Phys Biol, 4, 229-245.  
16102001 C.Q.Wenzel, C.Daniels, R.A.Keates, D.Brewer, and J.S.Lam (2005).
Evidence that WbpD is an N-acetyltransferase belonging to the hexapeptide acyltransferase superfamily and an important protein for O-antigen biosynthesis in Pseudomonas aeruginosa PAO1.
  Mol Microbiol, 57, 1288-1303.  
15044493 C.R.Sweet, A.H.Williams, M.J.Karbarz, C.Werts, S.R.Kalb, R.J.Cotter, and C.R.Raetz (2004).
Enzymatic synthesis of lipid A molecules with four amide-linked acyl chains. LpxA acyltransferases selective for an analog of UDP-N-acetylglucosamine in which an amine replaces the 3"-hydroxyl group.
  J Biol Chem, 279, 25411-25419.  
15333931 J.Gorman, and L.Shapiro (2004).
Structure of serine acetyltransferase from Haemophilus influenzae Rd.
  Acta Crystallogr D Biol Crystallogr, 60, 1600-1605.
PDB code: 1s80
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
12743100 J.M.Vilar, C.C.Guet, and S.Leibler (2003).
Modeling network dynamics: the lac operon, a case study.
  J Cell Biol, 161, 471-476.  
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 code is shown on the right.