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PDBsum entry 2ghr

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Transferase PDB id
2ghr
Jmol
Contents
Protein chain
269 a.a. *
Ligands
SO4
Waters ×78
* Residue conservation analysis
PDB id:
2ghr
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)
Resolution:
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
Date:
27-Mar-06     Release date:   11-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.46  - Homoserine O-succinyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
Succinyl-CoA
+ 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  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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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