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PDBsum entry 2rjs
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protein ligands Protein-protein interface(s) links
Isomerase PDB id
2rjs

 

 

 

 

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Contents
Protein chains
526 a.a. *
Ligands
296 ×2
Waters ×398
* Residue conservation analysis
PDB id:
2rjs
Name: Isomerase
Title: Sgtam bound to substrate mimic
Structure: Tyrosine aminomutase. Chain: a, b. Fragment: tyrosine aminomutase. Synonym: putative ammonia lyase/transferase. Engineered: yes
Source: Streptomyces globisporus. Organism_taxid: 1908. Gene: sgcc4. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.182     R-free:   0.245
Authors: T.J.Montavon,C.V.Christianson,S.D.Bruner
Key ref: T.J.Montavon et al. (2008). Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM. Bioorg Med Chem Lett, 18, 3099-3102. PubMed id: 18078753 DOI: 10.1016/j.bmcl.2007.11.046
Date:
15-Oct-07     Release date:   15-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8GMG0  (TAM_STRGL) -  MIO-dependent tyrosine 2,3-aminomutase from Streptomyces globisporus
Seq:
Struc: 		 
Seq:
Struc: 		539 a.a.
526 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: E.C.4.3.1.23  - tyrosine ammonia-lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosine = (E)-4-coumarate + NH4+
L-tyrosine
Bound ligand (Het Group name = 296)
matches with 70.59% similarity 		= (E)-4-coumarate
 + NH4(+)
      Cofactor: MIO
   Enzyme class 3: E.C.5.4.3.6  - tyrosine 2,3-aminomutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
L-tyrosine
 =
3-amino-3-(4-hydroxyphenyl)propanoate
Bound ligand (Het Group name = 296)
matches with 81.25% similarity
      Cofactor: MIO
Cobalamin
 Pyridoxal 5'-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2007.11.046 Bioorg Med Chem Lett 18:3099-3102 (2008)
PubMed id: 18078753  
 
 
Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.
T.J.Montavon, C.V.Christianson, G.M.Festin, B.Shen, S.D.Bruner.
 
  ABSTRACT  
 
The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20577998 H.A.Cooke, and S.D.Bruner (2010).
Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites.
  Biopolymers, 93, 802-810.
PDB codes: 3kdy 3kdz
20336235 Z.X.Liang (2010).
Complexity and simplicity in the biosynthesis of enediyne natural products.
  Nat Prod Rep, 27, 499-528.  
19123196 B.Wu, W.Szymanski, P.Wietzes, S.de Wildeman, G.J.Poelarends, B.L.Feringa, and D.B.Janssen (2009).
Enzymatic Synthesis of Enantiopure alpha- and beta-Amino Acids by Phenylalanine Aminomutase-Catalysed Amination of Cinnamic Acid Derivatives.
  Chembiochem, 10, 338-344.  
19620019 H.A.Cooke, C.V.Christianson, and S.D.Bruner (2009).
Structure and chemistry of 4-methylideneimidazole-5-one containing enzymes.
  Curr Opin Chem Biol, 13, 460-468.  
19551180 J.L.Meier, and M.D.Burkart (2009).
The chemical biology of modular biosynthetic enzymes.
  Chem Soc Rev, 38, 2012-2045.  
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 codes are shown on the right.

 

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