PDBsum entry: 1gy2

Electron transport

PDB id: 1gy2

Contents

Protein chains

155 a.a. *

Ligands

GOL

Metals

_CU ×2

Waters ×136

* Residue conservation analysis

PDB id:

1gy2

Name:

Electron transport

Title:

Crystal structure of met148leu rusticyanin

Structure:

Rusticyanin. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Thiobacillus ferrooxidans. Organism_taxid: 920. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.82Å R-factor: 0.184 R-free: 0.219

Authors:

M.A.Hough,L.D.Kanbi,S.Antonyuk,F.Dodd,S.Hasnain

Key ref:

L.D.Kanbi et al. (2002). Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins. J Mol Biol, 320, 263-275. PubMed id: 12079384 DOI: 10.1016/S0022-2836(02)00443-6

Date:

16-Apr-02 Release date: 23-May-02

Protein chains

P0C918  (RUS2_THIFE) -  Rusticyanin

Seq: 187 a.a.

Struc: 155 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: periplasmic space (1 term)
• Biological process: transport (2 terms)
• Biochemical function: electron carrier activity (3 terms)

DOI no: 10.1016/S0022-2836(02)00443-6

J Mol Biol 320:263-275 (2002)

PubMed id: 12079384

Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins.

L.D.Kanbi, S.Antonyuk, M.A.Hough, J.F.Hall, F.E.Dodd, S.S.Hasnain.

ABSTRACT

The crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin are presented at 1.82 and 1.65 A resolution, respectively. Both of these structures have two molecules in the asymmetric unit compared to the one present in the crystal form of the native protein. This provides an opportunity to investigate intramolecular electron transfer pathways in rusticyanin. The redox potential of the Met148Leu mutant ( approximately 800 mV) is elevated compared to that of the native protein ( approximately 670 mV at pH 3.2) while that of the Ser86Asp mutant ( approximately 623 mV at pH 3.2) is decreased. The effect of the Ser86Asp mutation on the hydrogen bonding near the type 1 Cu site is discussed and hence its role in determining acid stability is examined. The type 1 Cu site of Met148Leu mimics the structural and biochemical characteristics of those found in domain II of ceruloplasmin and fungal laccase. Moreover, the native rusticyanin's cupredoxin core and the type 1 Cu site closely resemble those found in ascorbate oxidase and nitrite reductase. Structure based phylogenetic trees have been re-examined in view of the additional structural data on rusticyanin and fungal laccase. We confirm that rusticyanin is in the same class as nitrite reductase domain 2, laccase domain 3 and ceruloplasmin domains 2, 4 and 6.

Selected figure(s)

Figure 1.
Figure 1. The 2F[o] -F[c] electron density contoured at 1s for (a) the Met148Leu type 1 Cu site and (b) around the mutated residue Asp86. 3s density is shown in red.

Figure 3.
Figure 3. The hydrogen bonding network around residue 86 for (a) native rusticyanin; (b) Ser86Asp rusticyanin.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2002, 320, 263-275) copyright 2002.

Figures were selected by an automated process.