6LVW
Polyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi
Summary for 6LVW
| Entry DOI | 10.2210/pdb6lvw/pdb |
| Descriptor | Beta-galactosidase Bga, ZINC ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | polyextremophilic enzyme, halophile, psychrophile, extremozyme, extremophile, sugar binding protein, hydrolase |
| Biological source | Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34) |
| Total number of polymer chains | 1 |
| Total formula weight | 78226.09 |
| Authors | Muhammad, R.,Arold, S.T. (deposition date: 2020-02-06, release date: 2020-10-28, Last modification date: 2023-11-29) |
| Primary citation | Karan, R.,Mathew, S.,Muhammad, R.,Bautista, D.B.,Vogler, M.,Eppinger, J.,Oliva, R.,Cavallo, L.,Arold, S.T.,Rueping, M. Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme. Microorganisms, 8:-, 2020 Cited by PubMed Abstract: The haloarchaeon is among the few polyextremophilic organisms capable of surviving in one of the most extreme aquatic environments on Earth, the Deep Lake of Antarctica (-18 °C to +11.5 °C and 21-28%, w/v salt content). Hence, has been proposed as a model for biotechnology and astrobiology to investigate potential life beyond Earth. To understand the mechanisms that allow proteins to adapt to both salinity and cold, we structurally (including X-ray crystallography and molecular dynamics simulations) and functionally characterized the β-galactosidase from (hla_bga). Recombinant hla_bga (produced in ) revealed exceptional stability, tolerating up to 4 M NaCl and up to 20% (v/v) of organic solvents. Despite being cold-adapted, hla_bga was also stable up to 60 °C. Structural analysis showed that hla_bga combined increased surface acidity (associated with halophily) with increased structural flexibility, fine-tuned on a residue level, for sustaining activity at low temperatures. The resulting blend enhanced structural flexibility at low temperatures but also limited protein movements at higher temperatures relative to mesophilic homologs. Collectively, these observations help in understanding the molecular basis of a dual psychrophilic and halophilic adaptation and suggest that such enzymes may be intrinsically stable and functional over an exceptionally large temperature range. PubMed: 33081237DOI: 10.3390/microorganisms8101594 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.493 Å) |
Structure validation
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