6lvw

Polyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi

spinqualitylabelsall models 6lvw, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lvw is a 1 chain structure with sequence from Halorubrum lacusprofundi ATCC 49239. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.493Å Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BGAL_HALLT Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in vitro. Publication Abstract from PubMed The haloarchaeon Halorubrum lacusprofundi 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 degrees C to +11.5 degrees C and 21-28%, w/v salt content). Hence, H. lacusprofundi 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 beta-galactosidase from H. lacusprofundi (hla_bga). Recombinant hla_bga (produced in Haloferax volcanii) 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 degrees 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. Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme.,Karan R, Mathew S, Muhammad R, Bautista DB, Vogler M, Eppinger J, Oliva R, Cavallo L, Arold ST, Rueping M Microorganisms. 2020 Oct 16;8(10). pii: microorganisms8101594. doi:, 10.3390/microorganisms8101594. PMID:33081237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase 3D structures

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