Crystal structures of the mycolic acid methyl transferase 1 (MmaA1) from Mycobacterium tuberculosis in the apo-form and in complex with different cofactors reveal unique features for substrate binding.

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Title: Crystal structures of the mycolic acid methyl transferase 1 (MmaA1) from Mycobacterium tuberculosis in the apo-form and in complex with different cofactors reveal unique features for substrate binding.
Authors: Chaudhary B; Structural and Molecular Biology Laboratory (SMBL), Department of Biotechnology, TERI School of Advanced Studies (TERI SAS), New Delhi, India.; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria., Kobakhidze G; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.; Vienna Biocenter PhD Program, a Doctoral School of the University of Vienna and the Medical University of Vienna, Vienna, Austria., Wachelder L; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.; Academy of Life Science and Technology, Avans University of Applied Sciences, Breda, Netherlands., Mazumdar PA; Independent Researcher, New Delhi, India., Dong G; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria., Madhurantakam C; Structural and Molecular Biology Laboratory (SMBL), Department of Biotechnology, TERI School of Advanced Studies (TERI SAS), New Delhi, India.
Source: Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2026 May; Vol. 44 (8), pp. 3713-3722. Date of Electronic Publication: 2025 Apr 09.
Publication Type: Journal Article
Journal Info: Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Crystal structures of the mycolic acid methyl transferase 1 (MmaA1) from Mycobacterium tuberculosis in the apo-form and in complex with different cofactors reveal unique features for substrate binding.
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  Data: <searchLink fieldCode="AU" term="%22Chaudhary+B%22">Chaudhary B</searchLink>; Structural and Molecular Biology Laboratory (SMBL), Department of Biotechnology, TERI School of Advanced Studies (TERI SAS), New Delhi, India.; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.<br /><searchLink fieldCode="AU" term="%22Kobakhidze+G%22">Kobakhidze G</searchLink>; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.; Vienna Biocenter PhD Program, a Doctoral School of the University of Vienna and the Medical University of Vienna, Vienna, Austria.<br /><searchLink fieldCode="AU" term="%22Wachelder+L%22">Wachelder L</searchLink>; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.; Academy of Life Science and Technology, Avans University of Applied Sciences, Breda, Netherlands.<br /><searchLink fieldCode="AU" term="%22Mazumdar+PA%22">Mazumdar PA</searchLink>; Independent Researcher, New Delhi, India.<br /><searchLink fieldCode="AU" term="%22Dong+G%22">Dong G</searchLink>; Max Perutz Labs, Vienna Biocenter, Medical University of Vienna, Vienna, Austria.<br /><searchLink fieldCode="AU" term="%22Madhurantakam+C%22">Madhurantakam C</searchLink>; Structural and Molecular Biology Laboratory (SMBL), Department of Biotechnology, TERI School of Advanced Studies (TERI SAS), New Delhi, India.
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  Data: <searchLink fieldCode="JN" term="%228404176%22">Journal of biomolecular structure & dynamics</searchLink> [J Biomol Struct Dyn] 2026 May; Vol. 44 (8), pp. 3713-3722. <i>Date of Electronic Publication: </i>2025 Apr 09.
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        Value: 10.1080/07391102.2025.2483952
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        StartPage: 3713
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      – TitleFull: Crystal structures of the mycolic acid methyl transferase 1 (MmaA1) from Mycobacterium tuberculosis in the apo-form and in complex with different cofactors reveal unique features for substrate binding.
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              Text: 2026 May
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