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PDBsum entry 1mli

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protein links
Intramolecular oxidoreductase PDB id
1mli
Jmol
Contents
Protein chains
(+ 4 more) 96 a.a.* *
* Residue conservation analysis
* C-alpha coords only
PDB id:
1mli
Name: Intramolecular oxidoreductase
Title: Crystal structure of muconolactone isomerase at 3.3 angstroms resolution
Structure: Muconolactone isomerase. Chain: a, b, c, d, e, f, g, h, i, j. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303
Biol. unit: Dodecamer (from PQS)
Resolution:
3.30Å     R-factor:   not given    
Authors: S.K.Katti,B.A.Katz,H.W.Wyckoff
Key ref: S.K.Katti et al. (1989). Crystal structure of muconolactone isomerase at 3.3 A resolution. J Mol Biol, 205, 557-571. PubMed id: 2926818
Date:
02-Nov-89     Release date:   15-Oct-90    
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00948  (CATC_PSEPU) -  Muconolactone Delta-isomerase
Seq:
Struc:
96 a.a.
96 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.3.3.4  - Muconolactone Delta-isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Benzoate Metabolism
      Reaction: (S)-5-oxo-2,5-dihydrofuran-2-acetate = 5-oxo-4,5-dihydrofuran-2-acetate
(S)-5-oxo-2,5-dihydrofuran-2-acetate
= 5-oxo-4,5-dihydrofuran-2-acetate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular aromatic compound metabolic process   3 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    Added reference    
 
 
J Mol Biol 205:557-571 (1989)
PubMed id: 2926818  
 
 
Crystal structure of muconolactone isomerase at 3.3 A resolution.
S.K.Katti, B.A.Katz, H.W.Wyckoff.
 
  ABSTRACT  
 
The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 A resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two alpha-helices and an antiparallel twisted beta-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
15965735 A.Ebihara, A.Okamoto, Y.Kousumi, H.Yamamoto, R.Masui, N.Ueyama, S.Yokoyama, and S.Kuramitsu (2005).
Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8.
  J Struct Funct Genomics, 6, 21-32.
PDB code: 1vdh
16049913 D.A.Sanders, J.R.Walker, T.Skarina, and A.Savchenko (2005).
The X-ray crystal structure of PA3566 from Pseudomonas aureginosa at 1.8 A resolution.
  Proteins, 61, 209-212.
PDB code: 1x7v
15779043 M.A.Willis, F.Song, Z.Zhuang, W.Krajewski, V.R.Chalamasetty, P.Reddy, A.Howard, D.Dunaway-Mariano, and O.Herzberg (2005).
Structure of YciI from Haemophilus influenzae (HI0828) reveals a ferredoxin-like alpha/beta-fold with a histidine/aspartate centered catalytic site.
  Proteins, 59, 648-652.
PDB code: 1mwq
12514126 G.Sciara, S.G.Kendrew, A.E.Miele, N.G.Marsh, L.Federici, F.Malatesta, G.Schimperna, C.Savino, and B.Vallone (2003).
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
  EMBO J, 22, 205-215.
PDB codes: 1lq9 1n5q 1n5s 1n5t 1n5v
12547421 V.Anantharaman, L.Aravind, and E.V.Koonin (2003).
Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins.
  Curr Opin Chem Biol, 7, 12-20.  
10336376 R.Schleif (1999).
Arm-domain interactions in proteins: a review.
  Proteins, 34, 1-3.  
  8990288 D.Eulberg, L.A.Golovleva, and M.Schlömann (1997).
Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP.
  J Bacteriol, 179, 370-381.  
8905091 C.S.Harwood, and R.E.Parales (1996).
The beta-ketoadipate pathway and the biology of self-identity.
  Annu Rev Microbiol, 50, 553-590.  
  7814330 J.E.Houghton, T.M.Brown, A.J.Appel, E.J.Hughes, and L.N.Ornston (1995).
Discontinuities in the evolution of Pseudomonas putida cat genes.
  J Bacteriol, 177, 401-412.  
2696175 N.Allewell (1989).
Evolving to dissimilate hydrocarbons.
  Trends Biochem Sci, 14, 473-474.  
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.