PDBsum entry 2ghr

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Transferase PDB id
Protein chain
269 a.a. *
Waters ×78
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of homoserine o-succinyltransferase (np_98 from bacillus cereus atcc 10987 at 2.40 a resolution
Structure: Homoserine o-succinyltransferase. Chain: a. Synonym: homoserine o- transsuccinylase, hts. Engineered: yes
Source: Bacillus cereus. Organism_taxid: 1396. Atcc: 10987. Gene: meta. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
2.40Å     R-factor:   0.191     R-free:   0.250
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
C.Zubieta et al. (2007). Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution. Proteins, 68, 999. PubMed id: 17546672 DOI: 10.1002/prot.21208
27-Mar-06     Release date:   11-Apr-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q72X44  (META_BACC1) -  Homoserine O-succinyltransferase
301 a.a.
269 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Homoserine O-succinyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
+ L-homoserine
= CoA
+ O-succinyl-L-homoserine
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  


DOI no: 10.1002/prot.21208 Proteins 68:999 (2007)
PubMed id: 17546672  
Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution.
C.Zubieta, S.S.Krishna, D.McMullan, M.D.Miller, P.Abdubek, S.Agarwalla, E.Ambing, T.Astakhova, H.L.Axelrod, D.Carlton, H.J.Chiu, T.Clayton, M.Deller, M.DiDonato, L.Duan, M.A.Elsliger, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, A.Kumar, D.Marciano, A.T.Morse, E.Nigoghossian, S.Oommachen, R.Reyes, C.L.Rife, H.van den Bedem, D.Weekes, A.White, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. Crystal structure of HTS from B. cereus. (A) Stereo ribbon diagram of HTS monomer color-coded from N-terminus (blue) to C-terminus (red). Helices (H1-H11) and -strands ( 1- 11) are indicated. The disordered region (75-86) is depicted by a grey dashed line. -sheets are indicated by a red A , A, and B. (B) Diagram showing the secondary structural elements of HTS superimposed on its primary sequence. The -helices, 3[10]-helices, -strands, -bulges, and -turns are indicated. The -hairpin is depicted as a red loop. Disordered regions are depicted by dashed regions with the corresponding sequence shown below.
Figure 2.
Figure 2. HTS dimer and structural comparisons with GMP synthase from Thermoplasma acidophilum (PDB accession code 2a9v). (A) Stereo view of the HTS dimer showing the N-terminal -strand exchange between the monomers, colored green and orange. The N- and C-termini are labeled. (B) Stereo overlay of the HTS monomer (grey) and GMP synthase from T. acidophilum (light green) with the proposed His-Glu-Cys catalytic triad in ball-and-stick representation. (C) Close-up view of the active sites of HTS and GMP synthase colored as per (B). Active site catalytic triad residues are depicted as ball-and-sticks and colored by atom type (N blue, S orange, O red, and C light green or grey). HTS residues are labeled, and corresponding GMP synthase residues are in parentheses.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 68, 999-0) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18216013 C.Zubieta, K.A.Arkus, R.E.Cahoon, and J.M.Jez (2008).
A single amino acid change is responsible for evolution of acyltransferase specificity in bacterial methionine biosynthesis.
  J Biol Chem, 283, 7561-7567.
PDB code: 2vdj
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