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Year : 2011  |  Volume : 2  |  Issue : 3  |  Page : 55  

Three-dimensional structure prediction of putative conserved proteins from R. rickettsiae: An approach to function annotation


Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi-110025, India

Date of Web Publication26-May-2012

Correspondence Address:
Sobia Zaidi
Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi-110025
India
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Source of Support: None, Conflict of Interest: None


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How to cite this article:
Zaidi S, Ahmad F, Hassan M. Three-dimensional structure prediction of putative conserved proteins from R. rickettsiae: An approach to function annotation. J Nat Sc Biol Med 2011;2, Suppl S1:55

How to cite this URL:
Zaidi S, Ahmad F, Hassan M. Three-dimensional structure prediction of putative conserved proteins from R. rickettsiae: An approach to function annotation. J Nat Sc Biol Med [serial online] 2011 [cited 2020 Jan 28];2, Suppl S1:55. Available from: http://www.jnsbm.org/text.asp?2011/2/3/55/95807

Rickettsia is a genus of motile, gram negative and non spore forming highly pleomorphic bacteria having many virulent genes. Due to these virulent genes, these bacteria causes many pathological disorders including, typhoid, Rickettsial pox, African tick bite fever, rocky mountain spotted fever, Australian tick typhus fever and many others. Certain segments of genome of these bacteria resemble mitochondrial genes. We have analyzed all gene products of Rickettsia rickettsiae and found that many genes are not annotated for their functions and therefore are categorised as hypothetical proteins. We annotated all these sequences of hypothetical proteins in order to propose their functions inside the cell. Our gene annotation analysis indicate that many hypothetical proteins have close resemblance to proteins with known functions such as transmembrane protein, ABC transporter, molecular chaperones and many enzymes such as membrane proteases, oxidoreductase, guanylate cyclase and beta lactamase. We successfully built the structural model for several proteins and analyzed their structure in order to propose their possible functions, based on conserved three-dimensional structure and motifs. Our structure and functional analysis will provide an insight for the molecular basis of pathogenesis.




 

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