PDBsum entry 3fca

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protein metals Protein-protein interface(s) links
Transferase PDB id
Protein chains
291 a.a. *
_ZN ×2
Waters ×164
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Genetic incorporation of a metal-ion chelating amino acid into proteins as biophysical probe
Structure: Cysteine synthase. Chain: a, b. Synonym: tm0665. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.15Å     R-factor:   0.209     R-free:   0.244
Authors: F.Wang,H.Lee,G.Spraggon,P.G.Schultz
Key ref: H.S.Lee et al. (2009). Genetic incorporation of a metal-ion chelating amino acid into proteins as a biophysical probe. J Am Chem Soc, 131, 2481-2483. PubMed id: 19193005
21-Nov-08     Release date:   17-Feb-09    
Go to PROCHECK summary

Protein chains
No UniProt id for this chain
Struc: 291 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Cysteine synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
+ 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     cysteine biosynthetic process from serine   1 term 
  Biochemical function     cysteine synthase activity     1 term  


J Am Chem Soc 131:2481-2483 (2009)
PubMed id: 19193005  
Genetic incorporation of a metal-ion chelating amino acid into proteins as a biophysical probe.
H.S.Lee, G.Spraggon, P.G.Schultz, F.Wang.
A metal-ion chelating amino acid, (8-hydroxyquinolin-3-yl)alanine, was genetically encoded in E. coli by an amber nonsense codon and corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. The amino acid was incorporated into TM0665 protein, and the mutant protein was cocrystallized with Zn(2+) to determine the structure by SAD phasing. The structure showed a high occupancy of the heavy metal bound to the HQ-Ala residue, and the heavy metal provided excellent phasing power to determine the structure. This method also facilitates the de novo design of metalloproteins with novel structures and functions, including fluorescent sensors.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21224416 A.K.Antonczak, Z.Simova, I.T.Yonemoto, M.Bochtler, A.Piasecka, H.Czapinska, A.Brancale, and E.M.Tippmann (2011).
Importance of single molecular determinants in the fidelity of expanded genetic codes.
  Proc Natl Acad Sci U S A, 108, 1320-1325.
PDB code: 3prh
21185770 E.M.Brustad, and F.H.Arnold (2011).
Optimizing non-natural protein function with directed evolution.
  Curr Opin Chem Biol, 15, 201-210.  
20307192 C.C.Liu, and P.G.Schultz (2010).
Adding new chemistries to the genetic code.
  Annu Rev Biochem, 79, 413-444.  
19669620 D.H.Jones, S.E.Cellitti, X.Hao, Q.Zhang, M.Jahnz, D.Summerer, P.G.Schultz, T.Uno, and B.H.Geierstanger (2010).
Site-specific labeling of proteins with NMR-active unnatural amino acids.
  J Biomol NMR, 46, 89.  
20150964 E.Young, and H.Alper (2010).
Synthetic biology: tools to design, build, and optimize cellular processes.
  J Biomed Biotechnol, 2010, 130781.  
20179771 F.Wang, S.Robbins, J.Guo, W.Shen, and P.G.Schultz (2010).
Genetic incorporation of unnatural amino acids into proteins in Mycobacterium tuberculosis.
  PLoS One, 5, e9354.  
20462377 G.Otting (2010).
Protein NMR using paramagnetic ions.
  Annu Rev Biophys, 39, 387-405.  
20411286 G.S.Sundaram, I.R.Morgan, and E.M.Tippmann (2010).
Synthesis of bioorthogonal and crosslinking amino acids for use in peptide synthesis.
  Amino Acids, 39, 1381-1384.  
20024068 N.Voloshchuk, and J.K.Montclare (2010).
Incorporation of unnatural amino acids for synthetic biology.
  Mol Biosyst, 6, 65-80.  
20147747 T.S.Young, and P.G.Schultz (2010).
Beyond the canonical 20 amino acids: expanding the genetic lexicon.
  J Biol Chem, 285, 11039-11044.  
19529883 X.C.Su, and G.Otting (2010).
Paramagnetic labelling of proteins and oligonucleotides for NMR.
  J Biomol NMR, 46, 101-112.  
  19856359 J.Guo, C.E.Melançon, H.S.Lee, D.Groff, and P.G.Schultz (2009).
Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids.
  Angew Chem Int Ed Engl, 48, 9148-9151.  
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 code is shown on the right.