Molecular Biology and Genetics

Electronic Journal of Biotechnology ISSN: 0717-3458 Vol. 6 No. 1, Issue of April 15, 2003
© 2003 by Universidad Católica de Valparaíso -- Chile Received June 26, 2002 / Accepted March 25, 2003
RESEARCH ARTICLE

A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei

Mohd. Firdaus Mohd. Raih
Centre for Gene Analysis and Technology
School of BioSciences and Biotechnology
Faculty of Science and Technology
Universiti Kebangsaan Malaysia
43600 UKM Bangi, Malaysia
Tel: +6 03 89267446
Fax: +6 03 89267972
E-mail: mfirr@cgat.ukm.my

Ahmad Tarmidi Sailan
Centre for Gene Analysis and Technology
School of BioSciences and Biotechnology
Faculty of Science and Technology
Universiti Kebangsaan Malaysia
43600 UKM Bangi, Malaysia
Tel: +6 03 89267446
Fax: +6 03 89267972
E-mail: tarmidi@medic.ukm.my

Zulkeflie Zamrod
Centre for Gene Analysis and Technology
School of BioSciences and Biotechnology
Faculty of Science and Technology
Universiti Kebangsaan Malaysia
43600 UKM Bangi, Malaysia
Tel: +6 03 89267446
Fax: +6 03 89267972
E-mail: zza@pkrisc.cc.ukm.my

Mohd. Noor Embi
Centre for Gene Analysis and Technology
School of BioSciences and Biotechnology
Faculty of Science and Technology
Universiti Kebangsaan Malaysia
43600 UKM Bangi, Malaysia
Tel: +6 03 89267446
Fax: +6 03 89267972
E-mail: noormb@pkrisc.cc.ukm.my

Rahmah Mohamed*
Centre for Gene Analysis and Technology
School of BioSciences and Biotechnology
Faculty of Science and Technology
Universiti Kebangsaan Malaysia
43600 UKM Bangi, Malaysia
Tel: +6 03 89267446
Fax: +6 03 89267972
E-mail: ram@cgat.ukm.my

http://cgat.ukm.my

* Corresponding author

Financial support: This work was funded by the Intensification of Research in Priority Areas (IRPA) grants IRPA 01-02-02-001 and IRPA-TOPDOWN 09-02-02-T001 provided by the Ministry of Science, Technology and the Environment, Malaysia.

Keywords: Burkholderia pseudomallei, cytochrome c oxidase, protein structure prediction, sequence alignments, structure-function extrapolation.

Acronyms:
Cox1: B. pseudomallei predicted cytochrome c oxidase subunit 1 protein;
Bp cox1: B. pseudomallei predicted cytocrome c oxidase subunit 1 gene;
SU: subunit;
ORF: open reading frame;
BLAST: Basic Local Alignment Search Tool;
TM: transmembrane;
TMH: transmembrane helices;
CVFF: consistent valence force field.
 

Abstract Full Text


Cytochrome c oxidase, the terminal enzyme of the respiratory chains of mitochondria and aerobic bacteria, catalyzes electron transfer from cytochrome c to molecular oxygen. The enzyme belongs to the haem-copper-containing oxidases superfamily. A recombinant plasmid carrying a 2.0 kb insert from a Burkholderia pseudomallei genomic library was subjected to automated DNA sequencing utilizing a primer walking strategy. Analysis of the 2002 bp insert revealed a 1536 bp open reading frame predicted to encode a putative cytochrome c oxidase. Further analysis using sequence alignments and tertiary structure analysis tools demonstrated that the hypothetical B. pseudomallei cytochrome c oxidase is similar to cytochrome c oxidases from other organisms such as Thermus thermophilus (36% protein sequence identity), Paracoccus denitrificans and bovine heart mitochondrial, the latter two which crystal structures available. The deduced 512 residue protein sequence includes the six canonical histidine residues involved in binding the low spin heme B and the binuclear center CuB/hemeA. The predicted tertiary structure of the hypothetical protein is consistent with previous models of electron transfer for cytochrome c oxidase.

 
Supported by UNESCO / MIRCEN network 
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