Proteins: Structure, Function, and Bioinformatics

Volume 80, Issue 4 pp. 1250-1257

Structure Note

Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH

Debajyoti Dutta,

Debajyoti Dutta

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

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Sudipta Bhattacharyya,

Sudipta Bhattacharyya

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

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Amit Kumar Das,

Corresponding Author

Amit Kumar Das

[email protected]

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, West Bengal, India===Search for more papers by this author

Debajyoti Dutta,

Debajyoti Dutta

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

Search for more papers by this author

Sudipta Bhattacharyya,

Sudipta Bhattacharyya

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

Search for more papers by this author

Amit Kumar Das,

Corresponding Author

Amit Kumar Das

[email protected]

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721032, West Bengal, India

Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, West Bengal, India===Search for more papers by this author

First published: 09 January 2012

https://doi.org/10.1002/prot.24024

Citations: 24

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Abstract

Crystal structure of Staphylococcal β-ketoacyl-ACP reductase 1 (SaFabG1) complexed with NADPH is determined at 2.5 Å resolution. The enzyme is essential in FAS-II pathway and utilizes NADPH to reduce β-ketoacyl-ACP to (S)-β-hydroxyacyl-ACP. Unlike the tetrameric FabGs, dimeric SaFabG1 shows positive homotropic cooperativity towards NADPH. Analysis of FabG:NADPH binary crystal structure endorses that NADPH interacts directly with the helices α4 and α5 those are present on a dimerization interface. A steady shift in tryptophan (of α4 helix) emission peak upon steady increment of NADPH concentration reveals that the dimeric interface is formed by α4-α4′ and α5-α5′ helices. This dimeric interface imparts positive homotropic cooperativity towards NADPH. PEG, a substrate mimicking molecule is also found near the active site of the enzyme. Proteins 2012; © 2011 Wiley Periodicals, Inc.

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Volume80, Issue4

April 2012

Pages 1250-1257

Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH

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Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH

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