3amr | pdb_00003amr

Crystal Structures of Bacillus subtilis Alkaline Phytase in Complex with Ca2+, Co2+, Ni2+, Mg2+ and myo-Inositol Hexasulfate

spinqualitylabelsall models 3amr, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3amr is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, IHS Related: 3ams Gene: phyC, phyB13 ("Vibrio subtilis" Ehrenberg 1835) Activity: 3-phytase, with EC number 3.1.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PHYC_BACIU] Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Only phytate, ADP, and ATP were hydrolyzed (100, 75, and 50% of the relative activity, respectively). Publication Abstract from PubMed Alkaline phytases from Bacillus species, which hydrolyze phytate to less phosphorylated myo-inositols and inorganic phosphate, have great potential as additives to animal feed. The thermostability and neutral optimum pH of Bacillus phytase are attributed largely to the presence of calcium ions. Nonetheless, no report has demonstrated directly how the metal ions coordinate phytase and its substrate to facilitate the catalytic reaction. In this study, the interactions between a phytate analog (myo-inositol hexasulfate) and divalent metal ions in Bacillus subtilis phytase were revealed by the crystal structure at 1.25 A resolution. We found all, except the first, sulfates on the substrate analog have direct or indirect interactions with amino acid residues in the enzyme active site. The structures also unraveled two active site-associated metal ions that were not explored in earlier studies. Significantly, one metal ion could be crucial to substrate binding. In addition, binding of the fourth sulfate of the substrate analog to the active site appears to be stronger than that of the others. These results indicate that alkaline phytase starts by cleaving the fourth phosphate, instead of the third or the sixth that were proposed earlier. Our high-resolution, structural representation of Bacillus phytase in complex with a substrate analog and divalent metal ions provides new insight into the catalytic mechanism of alkaline phytases in general. Crystal structures of Bacillus alkaline phytase in complex with divalent metal ions and inositol hexasulfate.,Zeng YF, Ko TP, Lai HL, Cheng YS, Wu TH, Ma Y, Chen CC, Yang CS, Cheng KJ, Huang CH, Guo RT, Liu JR J Mol Biol. 2011 Jun 3;409(2):214-24. Epub 2011 Apr 2. PMID:21463636 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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