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PDBsum entry 1j4j
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protein ligands Protein-protein interface(s) links
Transferase PDB id
1j4j

 

 

 

 

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Contents
Protein chains
170 a.a. *
Ligands
ACO ×2
Waters ×181
* Residue conservation analysis
PDB id:
1j4j
Name: Transferase
Title: Crystal structure of tabtoxin resistance protein (form ii) complexed with an acyl coenzyme a
Structure: Tabtoxin resistance protein. Chain: a, b. Synonym: acetyltransferase. Engineered: yes
Source: Pseudomonas syringae pv. Tabaci. Organism_taxid: 322. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.55Å     R-factor:   0.188     R-free:   0.254
Authors: H.He,Y.Ding,M.Bartlam,R.Zhang,N.Duke,A.Joachimiak,Y.Shao,Z.Cao, H.Tang,Y.Liu,F.Jiang,J.Liu,N.Zhao,Z.Rao
Key ref:
H.He et al. (2003). Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. J Mol Biol, 325, 1019-1030. PubMed id: 12527305 DOI: 10.1016/S0022-2836(02)01284-6
Date:
02-Oct-01     Release date:   03-Jun-03    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16966  (TTR_PSEAJ) -  Acetyltransferase from Pseudomonas amygdali pv. tabaci
Seq:
Struc: 		177 a.a.
170 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/S0022-2836(02)01284-6 J Mol Biol 325:1019-1030 (2003)
PubMed id: 12527305  
 
 
Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.
H.He, Y.Ding, M.Bartlam, F.Sun, Y.Le, X.Qin, H.Tang, R.Zhang, A.Joachimiak, J.Liu, N.Zhao, Z.Rao.
 
  ABSTRACT  
 
Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. AcCoA recognition and binding. (a) A stereo view of an |F[o]| -|F[c]| difference map calculated in the absence of AcCoA. The map is contoured at 2s. (b) The side-chain interactions between TTR and AcCoA. Hydrogen bonds are marked by green arrows and hydrophobic interactions are indicated in red. 		Figure 4.
Figure 4. (a) A stereo view of the catalytic site showing interactions between TTR and both AcCoA and the tightly bound water molecule; GRASP surfaces showing the AcCoA-binding pocket viewed from the front (b) and back (c), respectively (color coded according to electrostatic potential: blue corresponds to 20k[B]T; white, 0k[B]T; and red, -20k[B]T). (b) The front view, with two polar regions inside the hydrophobic-binding pocket. The positive region indicated in blue corresponds to residue Lys95 and the negative region in red corresponds to residues Glu92 and Asp130. (c) The back view.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2003, 325, 1019-1030) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20446033 E.Cundliffe, and A.L.Demain (2010).
Avoidance of suicide in antibiotic-producing microbes.
  J Ind Microbiol Biotechnol, 37, 643-672.  
19889644 K.Oda, Y.Matoba, M.Noda, T.Kumagai, and M.Sugiyama (2010).
Catalytic mechanism of bleomycin N-acetyltransferase proposed on the basis of its crystal structure.
  J Biol Chem, 285, 1446-1456.
PDB codes: 2zw4 2zw5 2zw6 2zw7
19493340 K.S.Makarova, Y.I.Wolf, and E.V.Koonin (2009).
Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes.
  Biol Direct, 4, 19.  
18184660 D.Shi, V.Sagar, Z.Jin, X.Yu, L.Caldovic, H.Morizono, N.M.Allewell, and M.Tuchman (2008).
The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.
  J Biol Chem, 283, 7176-7184.
PDB codes: 2r8v 2r98 3b8g
  18997321 M.W.Vetting, J.C.Errey, and J.S.Blanchard (2008).
Rv0802c from Mycobacterium tuberculosis: the first structure of a succinyltransferase with the GNAT fold.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 978-985.
PDB codes: 2vzy 2vzz
16495645 H.Kiyota (2006).
Synthesis of naturally derived bioactive compounds of agricultural interest.
  Biosci Biotechnol Biochem, 70, 317-324.  
16855251 M.N.Hung, E.Rangarajan, C.Munger, G.Nadeau, T.Sulea, and A.Matte (2006).
Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis.
  J Bacteriol, 188, 5606-5617.
PDB codes: 2fs5 2ft0
16835859 V.Simunovic, J.Zapp, S.Rachid, D.Krug, P.Meiser, and R.Müller (2006).
Myxovirescin A biosynthesis is directed by hybrid polyketide synthases/nonribosomal peptide synthetase, 3-hydroxy-3-methylglutaryl-CoA synthases, and trans-acting acyltransferases.
  Chembiochem, 7, 1206-1220.  
15695811 G.L.Card, N.A.Peterson, C.A.Smith, B.Rupp, B.M.Schick, and E.N.Baker (2005).
The crystal structure of Rv1347c, a putative antibiotic resistance protein from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests an alternative function in siderophore biosynthesis.
  J Biol Chem, 280, 13978-13986.
PDB code: 1yk3
15123251 M.W.Vetting, S.Magnet, E.Nieves, S.L.Roderick, and J.S.Blanchard (2004).
A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones.
  Chem Biol, 11, 565-573.
PDB codes: 1s3z 1s5k 1s60
14962386 S.Biarrotte-Sorin, A.P.Maillard, J.Delettré, W.Sougakoff, M.Arthur, and C.Mayer (2004).
Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition.
  Structure, 12, 257-267.
PDB codes: 1ne9 1p4n
15341646 S.Teichert, B.Schönig, S.Richter, and B.Tudzynski (2004).
Deletion of the Gibberella fujikuroi glutamine synthetase gene has significant impact on transcriptional control of primary and secondary metabolism.
  Mol Microbiol, 53, 1661-1675.  
15215527 Y.Ye, and A.Godzik (2004).
Database searching by flexible protein structure alignment.
  Protein Sci, 13, 1841-1850.  
12930994 M.W.Vetting, S.L.Roderick, M.Yu, and J.S.Blanchard (2003).
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.
  Protein Sci, 12, 1954-1959.
PDB codes: 1ozp 1p0h
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.

 

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