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PDBsum entry 1o58

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1o58
Jmol
Contents
Protein chains
293 a.a. *
266 a.a. *
Ligands
PO4 ×8
Waters ×937
* Residue conservation analysis
PDB id:
1o58
Name: Transferase
Title: Crystal structure of o-acetylserine sulfhydrylase (tm0665) f thermotoga maritima at 1.80 a resolution
Structure: O-acetylserine sulfhydrylase. Chain: a, b, c, d. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm0665. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
1.80Å     R-factor:   0.159     R-free:   0.198
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
A.Heine et al. (2004). Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution. Proteins, 56, 387-391. PubMed id: 15211522 DOI: 10.1002/prot.20003
Date:
20-Aug-03     Release date:   02-Sep-03    
Supersedes: 1j6n
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9WZD3  (Q9WZD3_THEMA) -  Cysteine synthase
Seq:
Struc:
291 a.a.
293 a.a.
Protein chains
Pfam   ArchSchema ?
Q9WZD3  (Q9WZD3_THEMA) -  Cysteine synthase
Seq:
Struc:
291 a.a.
266 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.2.5.1.47  - Cysteine synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
O-acetyl-L-serine
+ hydrogen sulfide
= L-cysteine
+ acetate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular amino acid biosynthetic process   3 terms 
  Biochemical function     transferase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1002/prot.20003 Proteins 56:387-391 (2004)
PubMed id: 15211522  
 
 
Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution.
A.Heine, J.M.Canaves, F.von Delft, L.S.Brinen, X.Dai, A.M.Deacon, M.A.Elsliger, S.Eshaghi, R.Floyd, A.Godzik, C.Grittini, S.K.Grzechnik, C.Guda, L.Jaroszewski, C.Karlak, H.E.Klock, E.Koesema, J.S.Kovarik, A.Kreusch, P.Kuhn, S.A.Lesley, D.McMullan, T.M.McPhillips, M.A.Miller, M.D.Miller, A.Morse, K.Moy, J.Ouyang, R.Page, A.Robb, K.Rodrigues, R.Schwarzenbacher, T.L.Selby, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, X.Wang, B.West, G.Wolf, K.O.Hodgson, J.Wooley, I.A.Wilson.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. A: Ribbon diagram of Thermotoga maritima TM0665 O-acetylserine sulfhydrylase color coded from N-terminus (blue) to C-terminus (red) showing the domain organization and location of the active site (arrow points towards bound phosphate). Helices (H1-H15) and -strands ( 1- 9) are indicated. The two phosphate molecules bound in the active site are shown in ball and stick. B: The TM0665 tetramer. C and D: Schematic representation of the interactions between TM0665 and the phosphate molecules bound to domain A (C) and domain B (D). Ligand bonds are in purple, protein amino acid bonds are in orange, and hydrogen-bonds are represented as dashed green lines with distances in A. Residues implicated in hydrophobic interactions are represented as barbed circle sections. The atoms are indicated as follows: carbon (black), nitrogen (blue), oxygen (red), phosphor (purple), and sulfur (yellow).
Figure 2.
Figure 2. A: Diagram showing the secondary structure elements in TM0665 superimposed on its primary sequence. The location of the -hairpin formed by -strands 1 and 2 is also depicted. B: Location of the phosphate 1 and phosphate 2 in the active site of TM0665 O-acetylserine sulfhydrylase. C: Location of pyridoxal 5 -phosphate (yellow) and methionine (magenta) in the catalytic site of O-acetylserine sulfhydrylase from Salmonella typhimurium (PDB: 1d6s).
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 56, 387-391) copyright 2004.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19640845 M.Goto, T.Yamauchi, N.Kamiya, I.Miyahara, T.Yoshimura, H.Mihara, T.Kurihara, K.Hirotsu, and N.Esaki (2009).
Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe.
  J Biol Chem, 284, 25944-25952.
PDB codes: 1wtc 2zr8
18214950 J.Deville, J.Rey, and M.Chabbert (2008).
Comprehensive analysis of the helix-X-helix motif in soluble proteins.
  Proteins, 72, 115-135.  
17894825 G.Zocher, U.Wiesand, and G.E.Schulz (2007).
High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli.
  FEBS J, 274, 5382-5389.
PDB code: 2v03
17064285 S.B.Conners, E.F.Mongodin, M.R.Johnson, C.I.Montero, K.E.Nelson, and R.M.Kelly (2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
  FEMS Microbiol Rev, 30, 872-905.  
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