6sc4

Gamma-Carbonic Anhydrase from the Haloarchaeon Halobacterium sp.

spinqualitylabelsall models 6sc4, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6sc4 is a 5 chain structure with sequence from Candidate division MSBL1 archaeon SCGC-AAA259I09. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: ACT, CD, NA, SO4, TRS, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A133ULQ3_9EURY Publication Abstract from PubMed Environments previously thought to be uninhabitable offer a tremendous wealth of unexplored microorganisms and enzymes. In this paper, we present the discovery and characterization of a novel gamma-carbonic anhydrase (gamma-CA) from the polyextreme Red Sea brine pool Discovery Deep (2141 m depth, 44.8 degrees C, 26.2% salt) by single-cell genome sequencing. The extensive analysis of the selected gene helps demonstrate the potential of this culture-independent method. The enzyme was expressed in the bioengineered haloarchaeon Halobacterium sp. NRC-1 and characterized by X-ray crystallography and mutagenesis. The 2.6 A crystal structure of the protein shows a trimeric arrangement. Within the gamma-CA, several possible structural determinants responsible for the enzyme's salt stability could be highlighted. Moreover, the amino acid composition on the protein surface and the intra- and intermolecular interactions within the protein differ significantly from those of its close homologs. To gain further insights into the catalytic residues of the gamma-CA enzyme, we created a library of variants around the active site residues and successfully improved the enzyme activity by 17-fold. As several gamma-CAs have been reported without measurable activity, this provides further clues as to critical residues. Our study reveals insights into the halophilic gamma-CA activity and its unique adaptations. The study of the polyextremophilic carbonic anhydrase provides a basis for outlining insights into strategies for salt adaptation, yielding enzymes with industrially valuable properties, and the underlying mechanisms of protein evolution. Crystal Structure and Active Site Engineering of a Halophilic gamma-Carbonic Anhydrase.,Vogler M, Karan R, Renn D, Vancea A, Vielberg MT, Grotzinger SW, DasSarma P, DasSarma S, Eppinger J, Groll M, Rueping M Front Microbiol. 2020 Apr 28;11:742. doi: 10.3389/fmicb.2020.00742. eCollection, 2020. PMID:32411108 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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