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PDBsum entry 2fno

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2fno
Jmol
Contents
Protein chains
239 a.a. *
Ligands
SCN ×4
Waters ×395
* Residue conservation analysis
PDB id:
2fno
Name: Transferase
Title: Crystal structure of a glutathione s-transferase (atu5508) f agrobacterium tumefaciens str. C58 at 2.00 a resolution
Structure: Agr_pat_752p. Chain: a, b. Engineered: yes
Source: Agrobacterium tumefaciens. Organism_taxid: 176299. Strain: str. C58. Gene: 15162326. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.183     R-free:   0.219
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
M.Kosloff et al. (2006). Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution. Proteins, 65, 527-537. PubMed id: 16988933 DOI: 10.1002/prot.21130
Date:
11-Jan-06     Release date:   14-Feb-06    
Supersedes: 1zgm
PROCHECK
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 Headers
 References

Protein chains
Pfam  
Q7D2W7  (Q7D2W7_AGRT5) -  Glutathione S-transferase
Seq:
Struc:
232 a.a.
239 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     transferase activity     1 term  

 

 
DOI no: 10.1002/prot.21130 Proteins 65:527-537 (2006)
PubMed id: 16988933  
 
 
Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution.
M.Kosloff, G.W.Han, S.S.Krishna, R.Schwarzenbacher, M.Fasnacht, M.A.Elsliger, P.Abdubek, S.Agarwalla, E.Ambing, T.Astakhova, H.L.Axelrod, J.M.Canaves, D.Carlton, H.J.Chiu, T.Clayton, M.DiDonato, L.Duan, J.Feuerhelm, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, L.Jaroszewski, K.K.Jin, H.Johnson, H.E.Klock, M.W.Knuth, E.Koesema, A.Kreusch, P.Kuhn, I.Levin, D.McMullan, M.D.Miller, A.T.Morse, K.Moy, E.Nigoghossian, L.Okach, S.Oommachen, R.Page, J.Paulsen, K.Quijano, R.Reyes, C.L.Rife, E.Sims, G.Spraggon, V.Sridhar, R.C.Stevens, H.van den Bedem, J.Velasquez, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.
 
  ABSTRACT  
 
Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Dimerization of atGST1: (A) Stereo diagram of the hydrophobic key (Phe56) and lock (Leu97, lle101, Ala105, Trp136, lle139, Phe140, and Thr143) motif. The atGST1 lock-and-key motif is shown superimposed on the corresponding regions from -GST (6gsv). The ligand in the active site of 6gsv, (9S,10S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene (GPS) is shown in ball-and-stick. The atGST1 dimer is colored in forest green and blue, while the -GST dimer is colored in grey and pink. (B) Stereo diagram of the biologically relevant dimer of atGST1, color-coded from N-terminus (blue) to C-terminus (red).
Figure 4.
Figure 4. GST class-specific motifs shown in the context of a multiple-structure alignment of representative GSTs. Stereo representations of the C[ ]trace of atGST1 is colored red and all other GSTs are shown in grey. The seven motifs that define the various GST classes are labeled: (I) N catalytic tyrosine (ball-and-stick, orange), (II) mu loop (cyan), (III) hydrophobic Key (ball-and-stick, magenta), (IV) SNAIL/TRAIL motif (grey helix), (V) catalytic Asp that binds glutathione across the dimer interface (ball-and-stick, red), (VI) catalytic histidine (ball-and-stick, blue), and (VII) C' extension (C[ ]trace, magenta). For clarity, the corresponding motifs, when present in atGST1, are shown in forest green and arrows indicate the general positions of these motifs.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 65, 527-537) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19016852 N.Allocati, L.Federici, M.Masulli, and C.Di Ilio (2009).
Glutathione transferases in bacteria.
  FEBS J, 276, 58-75.  
  18259055 W.Garcia, R.F.Travensolo, N.C.Rodrigues, J.R.Muniz, C.S.Caruso, E.G.Lemos, A.P.Araujo, and E.Carrilho (2008).
Crystallization and preliminary X-ray diffraction analysis of a glutathione S-transferase from Xylella fastidiosa.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 85-87.  
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