Title
3d Structure Modeling Of A Transmembrane Protein, Fatty Acid Elongase
Abstract
Fatty acid elongase is an enzyme responsible for fatty acid chain elongation, a key step in synthesis of long chain fatty acids, including polyunsaturated fatty acids (PUFAs). Currently, the increasing demand has raised the interest in obtaining these PUFAs from alternative sources, e.g. filamentous fungi that are more economical and sustainable. To date, many research on primary structures of fatty acid elongases ELO family, including fugal elongases, revealed several conserved motifs. However, molecular mechanism for their functions is still unclear. In addition to experimental study, computational analysis of elongase structures may provide more insight into their substrate specificities and mechanisms of fatty acid chain elongation. Thus, this work proposes a 3D structural model of elongase of Mortierella alpina (BAF97073). This fungal elongase has been reported to be a PUFA-specific elongation enzyme. The model was built by an ab initio membrane-modeling application using ROSETTA 3.1, and was then refined by molecular dynamic simulation. The 7-transmembrane helices of the constructed model folds into an anti-parallel configuration and embeds in the lipid bilayer. The model reveals that all four conserved signature motifs of fatty acid elongase enzymes are located within the juxta-cytosolic transmembrane helix regions. This work also suggests a modeling strategy of this elongase structural model that can be applied to model other transmembrane proteins.
Year
DOI
Venue
2010
10.1007/978-3-642-16750-8_4
COMPUTATIONAL SYSTEMS-BIOLOGY AND BIOINFORMATICS
Keywords
Field
DocType
PUFAs, Fatty Acid Elongase, Transmembrane Protein, ab initio Modeling, ROSETTA
Transmembrane domain,Fatty acid,Enzyme,Biology,Biochemistry,Transmembrane protein,Lipid bilayer,Helix,Elongase,Polyunsaturated fatty acid
Conference
Volume
ISSN
Citations 
115
1865-0929
0
PageRank 
References 
Authors
0.34
7
5