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Title

Structure prediction and evolution of a halo-acid dehalogenase of Burkholderia mallei

 

Authors

Alok R Rai1*, Raghvendra Pratap Singh2, Alok Kumar Srivastava2 & Ramesh Chandra Dubey3

 

Affiliation

1Department of Microbiology, Seth Kesarimal Porwal College, Kamptee Maharashtra 441002, India; 2National Bureau of Agriculturally Important Microorganisms (ICAR), Kushmaur, Kaithauli, Mau Nath Bhanjan, Uttar Pradesh-275101, India; 3Department of Botany and Microbiology, Gurukul Kangri University, Haridwar, Uttrakhand-249404, India.

 

Email

raialok@sify.com; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received November 03, 2012; Accepted November 05, 2012; Published November 13, 2012

Abstract

Environmental pollutants containing halogenated organic compounds e.g. haloacid, can cause a plethora of health problems. The structural and functional analyses of the gene responsible of their degradation are an important aspect for environmental studies and are important to human well-being. It has been shown that some haloacids are toxic and mutagenic. Microorganisms capable of degrading these haloacids can be found in the natural environment. One of these, a soil-borne Burkholderia mallei posses the ability to grow on monobromoacetate (MBA). This bacterium produces a haloacid dehalogenase that allows the cell to grow on MBA, a highly toxic and mutagenic environmental pollutant. For the structural and functional analysis, a 346 amino acid encoding protein sequence of haloacid dehalogenase is retrieve from NCBI data base. Primary and secondary structure analysis suggested that the high percentage of helices in the structure makes the protein more flexible for folding, which might increase protein interactions. The consensus protein sub-cellular localization predictions suggest that dehalogenase protein is a periplasmic protein 3D2GO server, suggesting that it is mainly employed in metabolic process followed by hydrolase activity and catalytic activity. The tertiary structure of protein was predicted by homology modeling. The result suggests that the protein is an unstable protein which is also an important characteristic of active enzyme enabling them to bind various cofactors and substrate for proper functioning. Validation of 3D structure was done using Ramachandran plot ProsA-web and RMSD score. This predicted information will help in better understanding of mechanism underlying haloacid dehalogenase encoding protein and its evolutionary relationship.

 

Keywords

Burkholderia mallei, haloacid dehalognease, homology modeling

 

Citation

Rai et al. Bioinformation 8(22): 1111-1113 (2012)

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.