Designed di-heme binding helical transmembrane protein

De novo designing of functional membrane proteins is fundamental in terms of understanding the structure, folding, and stability of membrane proteins. In this work, we report the design and characterization of a transmembrane protein, termed HETPRO (HEme-binding Transmembrane PROtein), that binds tw...

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Main Authors: Mahajan, Mukesh, Bhattacharjya, Surajit
Other Authors: School of Biological Sciences
Format: Journal Article
Language:English
Published: 2014
Subjects:
Online Access:https://hdl.handle.net/10356/105143
http://hdl.handle.net/10220/20460
http://dx.doi.org/10.1002/cbic.201402142
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author Mahajan, Mukesh
Bhattacharjya, Surajit
author2 School of Biological Sciences
author_facet School of Biological Sciences
Mahajan, Mukesh
Bhattacharjya, Surajit
author_sort Mahajan, Mukesh
collection NTU
description De novo designing of functional membrane proteins is fundamental in terms of understanding the structure, folding, and stability of membrane proteins. In this work, we report the design and characterization of a transmembrane protein, termed HETPRO (HEme-binding Transmembrane PROtein), that binds two molecules of heme in a membrane and catalyzes oxidation/reduction reactions. The primary structure of HETPRO has been optimized in a guided fashion, from an antimicrobial peptide, for transmembrane orientation, defined 3D structure, and functions. HETPRO assembles into a tetrameric form, from an apo dimeric helical structure, in complex with cofactor in detergent micelles. The NMR structure of the apo HETPRO in micelles reveals an antiparallel helical dimer that inserts into the nonpolar core of detergent micelles. The well-defined structure of HETPRO and its ability to bind to heme moieties could be utilized to develop a functional membrane protein mimic for electron transport and photosystems.
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spelling ntu-10356/1051432019-12-06T21:46:29Z Designed di-heme binding helical transmembrane protein Mahajan, Mukesh Bhattacharjya, Surajit School of Biological Sciences DRNTU::Science::Biological sciences De novo designing of functional membrane proteins is fundamental in terms of understanding the structure, folding, and stability of membrane proteins. In this work, we report the design and characterization of a transmembrane protein, termed HETPRO (HEme-binding Transmembrane PROtein), that binds two molecules of heme in a membrane and catalyzes oxidation/reduction reactions. The primary structure of HETPRO has been optimized in a guided fashion, from an antimicrobial peptide, for transmembrane orientation, defined 3D structure, and functions. HETPRO assembles into a tetrameric form, from an apo dimeric helical structure, in complex with cofactor in detergent micelles. The NMR structure of the apo HETPRO in micelles reveals an antiparallel helical dimer that inserts into the nonpolar core of detergent micelles. The well-defined structure of HETPRO and its ability to bind to heme moieties could be utilized to develop a functional membrane protein mimic for electron transport and photosystems. 2014-09-08T08:05:08Z 2019-12-06T21:46:29Z 2014-09-08T08:05:08Z 2019-12-06T21:46:29Z 2014 2014 Journal Article Mahajan, M., & Bhattacharjya, S. (2014). Designed di-heme binding helical transmembrane protein. ChemBioChem, 15(9), 1257-1262. 1439-4227 https://hdl.handle.net/10356/105143 http://hdl.handle.net/10220/20460 http://dx.doi.org/10.1002/cbic.201402142 en ChemBioChem © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
spellingShingle DRNTU::Science::Biological sciences
Mahajan, Mukesh
Bhattacharjya, Surajit
Designed di-heme binding helical transmembrane protein
title Designed di-heme binding helical transmembrane protein
title_full Designed di-heme binding helical transmembrane protein
title_fullStr Designed di-heme binding helical transmembrane protein
title_full_unstemmed Designed di-heme binding helical transmembrane protein
title_short Designed di-heme binding helical transmembrane protein
title_sort designed di heme binding helical transmembrane protein
topic DRNTU::Science::Biological sciences
url https://hdl.handle.net/10356/105143
http://hdl.handle.net/10220/20460
http://dx.doi.org/10.1002/cbic.201402142
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