3WBH: Structural Characteristics Of Alkaline Phosphatase From A Moderately Halophilic Bacteria Halomonas Sp.593

Citation:
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 A 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 beta-sheet core with 19 surrounding alpha-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(alpha) r.m.s.d. of 0.82 A 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.
PDB ID: 3WBHDownload
MMDB ID: 118164
PDB Deposition Date: 2013/5/17
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3WBH: dimeric; determined by author and by software (PISA)
Molecular Components in 3WBH
Label Count Molecule
Proteins (2 molecules)
2
Alkaline Phosphatase
Molecule annotation
Chemicals (12 molecules)
1
6
2
4
3
2
* Click molecule labels to explore molecular sequence information.

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