Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis

Thinh-Phat Cao; Joong-Su Kim; Mi-Hee Woo; Jin Myung Choi; Youngsoo Jun; Kun Ho Lee; Sung Haeng Lee

doi:10.1007/s12275-016-6029-4

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Research Support, Non-U.S. Gov't
Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis: Thinh-Phat Cao ^1,2, Joong-Su Kim ³, Mi-Hee Woo ³, Jin Myung Choi ^1,4, Youngsoo Jun ^4,5, Kun Ho Lee ^2,6, Sung Haeng Lee ¹; Journal of Microbiology 2016;54(4):311-321.
DOI: https://doi.org/10.1007/s12275-016-6029-4
Published online: April 1, 2016

¹Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 501-759, Republic of Korea, ²National Research Center for Dementia, Chosun University, Gwangju 61452, Republic of Korea, ³Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, Jeongeup 580-185, Republic of Korea, ⁴School of Life Sciences and Silver Health Bio Research Center, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea, ⁵School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea, ⁶Department of Biomedical Science, Chosun University, Gwangju 61452, Republic of Korea¹Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 501-759, Republic of Korea, ²National Research Center for Dementia, Chosun University, Gwangju 61452, Republic of Korea, ³Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, Jeongeup 580-185, Republic of Korea, ⁴School of Life Sciences and Silver Health Bio Research Center, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea, ⁵School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea, ⁶Department of Biomedical Science, Chosun University, Gwangju 61452, Republic of Korea

Corresponding author: Sung Haeng Lee , Tel: +82-62-230-6381,

Received: 21 January 2016 • Revised: 2 March 2016 • Accepted: 3 March 2016

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Abstract

2-deoxyribose-5-phosphate aldolase (DERA) is a class I aldolase that catalyzes aldol condensation of two aldehydes in the active site, which is particularly germane in drug manufacture. Structural and biochemical studies have shown that the active site of DERA is typically loosely packed and displays broader substrate specificity despite sharing conserved folding architecture with other aldolases. The most distinctive structural feature of DERA compared to other aldolases is short and flexible C-terminal region. This region is also responsible for substrate recognition. Therefore, substrate tolerance may be related to the C-terminal structural features of DERA. Here, we determined the crystal structures of full length and C-terminal truncated DERA from Streptococcus suis (SsDERA). In common, both contained the typical (α/β)8 TIM-barrel fold of class I aldolases. Surprisingly, C-terminal truncation
result
ing in missing the last α9 and β8 secondary elements, allowed DERA to maintain activity comparable to the fulllength enzyme. Specifically, Arg186 and Ser205 residues at the C-terminus appeared mutually supplemental or less indispensible for substrate phosphate moiety recognition. Our results suggest that DERA might adopt a shorter C-terminal region than conventional aldolases during evolution pathway, resulting in a broader range of substrate tolerance through active site flexibility.

Keywords: 2-deoxyribose-5-phosphate aldolase;Class I aldolase;TIM-barrel;S. suis;DERA

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Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis

J. Microbiol. 2016;54(4):311-321. Published online April 1, 2016

DOI: https://doi.org/10.1007/s12275-016-6029-4

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