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R. Rahisuddin

As seen in: Cell Press, The Journal of Biological Chemistry
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Articles by R. Rahisuddin

Structural insights into the assembly and regulation of 2′-O RNA methylation by SARS-CoV-2 nsp16/nsp10

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By Anurag Misra, R. Rahisuddin, Manish Parihar, Shailee Arya, Thiruselvam Viswanathan, Nathaniel Jackson, Shan Qi, Siu-Hong Chan, Reuben S. Harris, Luis Martinez-Sobrido, Yogesh Gupta Verified
| Cell Press Verified
Keywords RNA methylation Nsp16 Nsp10 RNA capping Introduction Coronaviruses (CoVs) modify 2′-OH of ribose sugar of the first transcribed nucleotide (N1) to protect their mRNA from degradation and host innate immune recognition.1 The N1 base (usually A1 in CoVs, A1/G1 in other RNA viruses) is enzymatically modified with the sequential attachment of an RNA cap and its subsequent methylation by S-adenosyl-L-methionine (SAM)-dependent methyltransferases.2,3 The capping of SARS-CoV-2 mRNA includes...
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Desolvation of Peptide Bond by O to S Substitution Impacts Protein Stability

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By Bhavesh Khatri, Shampa Raghunathan, Sohini Chakraborti, R. Rahisuddin
| Wiley Online Library Verified
Communication Dr. Bhavesh Khatri, orcid.org/0000-0002-3603-7839 Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012 India Search for more papers by this author Dr. Shampa Raghunathan, Center for Computational Natural Sciences and Bioinformatics, International Institute of Information Technology, Hyderabad, 500032 India Present Address: École Centrale School of Engineering, Mahindra University, Hyderabad, 500043 India Search for more papers by this author Sohini...
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Molecular Mechanism of Selective Substrate Engagement and Inhibitor Dis-engagement of Cysteine Synthase

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By Abhishek Kaushik, Neha Saini, Ravi Singh, R. Rahisuddin
| The Journal of Biological Chemistry Verified
Abstract O-acetyl serine sulfhydrylase (OASS), referred to as Cysteine Synthase (CS), synthesizes cysteine from O-acetyl serine (OAS) and sulfur in bacteria and plants. The inherent challenge for CS is to overcome 4-6 log-folds stronger affinity for its natural inhibitor, serine acetyltransferase (SAT), as compared to its affinity for substrate, OAS.
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