6P3L
Crystal Structure of Ketosteroid Isomerase from Mycobacterium hassiacum (mhKSI)
Summary for 6P3L
| Entry DOI | 10.2210/pdb6p3l/pdb |
| Descriptor | SnoaL-like domain protein, SULFATE ION, GUANIDINE, ... (4 entities in total) |
| Functional Keywords | isomerase, thermophile |
| Biological source | Mycobacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) |
| Total number of polymer chains | 2 |
| Total formula weight | 27698.74 |
| Authors | Yabukarski, F.,Doukov, T.,Pinney, M.,Herschlag, D. (deposition date: 2019-05-23, release date: 2020-05-27, Last modification date: 2024-03-13) |
| Primary citation | Pinney, M.M.,Mokhtari, D.A.,Akiva, E.,Yabukarski, F.,Sanchez, D.M.,Liang, R.,Doukov, T.,Martinez, T.J.,Babbitt, P.C.,Herschlag, D. Parallel molecular mechanisms for enzyme temperature adaptation. Science, 371:-, 2021 Cited by PubMed Abstract: The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation. PubMed: 33674467DOI: 10.1126/science.aay2784 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.571 Å) |
Structure validation
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