PDBsum entry 1gn2

Oxidoreductase

PDB id

1gn2

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Contents

			Protein chains

					(+ 2 more) 198 a.a. *

			Metals

					_FE ×8

* Residue conservation analysis

PDB id:

1gn2

Links

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

	Headers

	References

Protein chains

P9WGE7 (SODF_MYCTU) - Superoxide dismutase [Fe] from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: Struc:					207 a.a. 198 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class:

E.C.1.15.1.1 - superoxide dismutase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

2 superoxide + 2 H⁺ = H2O2 + O2

2 × superoxide	+	2 × H(+)	=	H2O2	+	O2

Cofactor:

Fe cation or Mn(2+) or (Zn(2+) and Cu cation)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

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.