spacer
spacer

PDBsum entry 1gn2

Go to PDB code: 
protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
1gn2
Jmol
Contents
Protein chains
(+ 2 more) 198 a.a. *
Metals
_FE ×8
* Residue conservation analysis
PDB id:
1gn2
Name: Oxidoreductase
Title: S123c mutant of the iron-superoxide dismutase from mycobacterium tuberculosis.
Structure: Superoxide dismutase. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Expressed in: mycobacterium vaccae. Expression_system_taxid: 1810
Biol. unit: Tetramer (from PDB file)
Resolution:
3.40Å     R-factor:   0.249     R-free:   0.270
Authors: K.A.Bunting,J.B.Cooper,I.J.Tickle,D.B.Young
Key ref: K.A.Bunting et al. (2002). Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis. Arch Biochem Biophys, 397, 69-76. PubMed id: 11747311 DOI: 10.1006/abbi.2001.2635
Date:
02-Oct-01     Release date:   05-Oct-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
P9WGE6  (SODF_MYCTO) -  Superoxide dismutase [Fe]
Seq:
Struc:
207 a.a.
198 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     3 terms  

 

 
DOI no: 10.1006/abbi.2001.2635 Arch Biochem Biophys 397:69-76 (2002)
PubMed id: 11747311  
 
 
Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis.
K.A.Bunting, J.B.Cooper, I.J.Tickle, D.B.Young.
 
  ABSTRACT  
 
With the aim of enhancing interactions involved in dimer formation, an intersubunit disulfide bridge was engineered in the superoxide dismutase enzyme of Mycobacterium tuberculosis. Ser-123 was chosen for mutation to cysteine since it resides at the dimer interface where the serine side chain interacts with the same residue in the opposite subunit. Gel electrophoresis and X-ray crystallographic studies of the expressed mutant confirmed formation of the disulfide bond under nonreducing conditions. However, the mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride. Decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18841998 M.M.Whittaker, and J.W.Whittaker (2008).
Conformationally gated metal uptake by apomanganese superoxide dismutase.
  Biochemistry, 47, 11625-11636.  
18829763 R.Mateo, E.Luna, V.Rincón, and M.G.Mateu (2008).
Engineering viable foot-and-mouth disease viruses with increased thermostability as a step in the development of improved vaccines.
  J Virol, 82, 12232-12240.  
17912757 R.Wintjens, D.Gilis, and M.Rooman (2008).
Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence.
  Proteins, 70, 1564-1577.  
16807887 J.L.Pellequer, and S.W.Chen (2006).
Multi-template approach to modeling engineered disulfide bonds.
  Proteins, 65, 192-202.  
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.