Dataset Information

Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593.

ABSTRACT: Alkaline phosphatase (AP) from the moderate halophilic bacterium Halomonas sp. 593 (HaAP) catalyzes the hydrolysis of phosphomonoesters over a wide salt-concentration range (1-4?M NaCl). In order to clarify the structural basis of its halophilic characteristics and its wide-range adaptation to salt concentration, the tertiary structure of HaAP was determined by X-ray crystallography to 2.1?Å resolution. The unit cell of HaAP contained one dimer unit corresponding to the biological unit. The monomer structure of HaAP contains a domain comprised of an 11-stranded ?-sheet core with 19 surrounding ?-helices similar to those of APs from other species, and a unique `crown' domain containing an extended `arm' structure that participates in formation of a hydrophobic cluster at the entrance to the substrate-binding site. The HaAP structure also displays a unique distribution of negatively charged residues and hydrophobic residues in comparison to other known AP structures. AP from Vibrio sp. G15-21 (VAP; a slight halophile) has the highest similarity in sequence (70.0% identity) and structure (C(?) r.m.s.d. of 0.82?Å for the monomer) to HaAP. The surface of the HaAP dimer is substantially more acidic than that of the VAP dimer (144 exposed Asp/Glu residues versus 114, respectively), and thus may enable the solubility of HaAP under high-salt conditions. Conversely, the monomer unit of HaAP formed a substantially larger hydrophobic interior comprising 329 C atoms from completely buried residues, whereas that of VAP comprised 264 C atoms, which may maintain the stability of HaAP under low-salt conditions. These characteristics of HaAP may be responsible for its unique functional adaptation permitting activity over a wide range of salt concentrations.

SUBMITTER: Arai S

PROVIDER: S-EPMC3949524 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593.

Arai Shigeki S Yonezawa Yasushi Y Ishibashi Matsujiro M Matsumoto Fumiko F Adachi Motoyasu M Tamada Taro T Tokunaga Hiroko H Blaber Michael M Tokunaga Masao M Kuroki Ryota R

Acta crystallographica. Section D, Biological crystallography 20140222 Pt 3

Alkaline phosphatase (AP) from the moderate halophilic bacterium Halomonas sp. 593 (HaAP) catalyzes the hydrolysis of phosphomonoesters over a wide salt-concentration range (1-4 M NaCl). In order to clarify the structural basis of its halophilic characteristics and its wide-range adaptation to salt concentration, the tertiary structure of HaAP was determined by X-ray crystallography to 2.1 Å resolution. The unit cell of HaAP contained one dimer unit corresponding to the biological unit. The mono ...[more]

PMID: 24598750

Similar Datasets

Project description:Two Gram-positive, rod-shaped moderately halophilic bacterial strains, designated AD7-25(T) and AB-11, were isolated from Aiding and Manasi salt lakes in Xinjiang of China, respectively. The strains were found to be able to grow at NaCl concentrations of 0-21 % (w/v), with optimum growth occurring at 6-8 % (w/v) NaCl. The optimal temperature and pH for growth were determined to be 33-37 °C and pH 7.0-7.5. Cells of the strains are motile by means of polar flagella. Both strains can produce ellipsoidal spores. The major cellular fatty acids were identified as anteiso-C15:0, iso-C15:0, iso-C14:0, anteiso-C17:0 and iso-C16:0. The diamino acid in the peptidoglycan and the major quinone system were determined to be meso-diaminopimelic acid (meso-DAP) and MK-7, respectively. The DNA G+C contents of stains AD7-25(T) and AB-11 were 39.8 and 40.0 mol%, respectively. Phylogenetic analysis based on 16S rRNA gene sequences revealed that these two novel strains are closely related to the genus Oceanobacillus showing 90-99.5 % similarity with respect to type strains. These two novel strains were most closely related to Oceanobacillus oncorhynchi subsp. incaldanensis DSM 16557(T) (99.1 and 99.5 %), followed by O. oncorhynchi subsp. oncorhynchi JCM 12661(T) (99.1 and 99.4 %), Oceanobacillus neutriphilus CGMCC 1.7693(T) (97.0 and 97.5 %), Oceanobacillus sojae JCM 15792(T) (97.6 and 98.0 %) and Oceanobacillus locisalsi KCTC 13253(T) (96.5 and 96.9 %). The DNA-DNA hybridization data indicated that DNA relatedness between strains AD7-25(T) and AB-11 was 91.0 %, and the genomic homology of representative strain AD7-25(T) with O. oncorhynchi subsp. incaldanensis DSM 16557(T), O. oncorhynchi subsp. oncorhynchi JCM 12661(T), O. neutriphilus CGMCC 1.7693(T), O. sojae JCM 15792(T) and O. locisalsi KCTC 13253(T) were 41, 39, 20, 23 and 17 %, respectively. On the basis of phenotypic and phylogenetic distinctiveness, strains AD7-25(T) and AB-11 should be assigned to the genus Oceanobacillus as a new species, for which the name Oceanobacillus aidingensis sp. nov. was proposed. The type strain is AD7-25(T) (=CGMCC 1.9106 (T) = NBRC 105904(T)).

Dataset Information

Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593.

Publications

Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets