4A9X

Pseudomonas fluorescens PhoX in complex with the substrate analogue AppCp

Summary for 4A9X

• Entry DOI: 10.2210/pdb4a9x/pdb
• Related: 3ZWU 4A9V
• Descriptor: PHOX, 1,2-ETHANEDIOL, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (6 entities in total)
• Functional Keywords: hydrolase, beta-propeller
• Biological source: PSEUDOMONAS FLUORESCENS
• Total number of polymer chains: 1
• Total formula weight: 65510.81

Authors

Yong, S.C.,Roversi, P.,Lillington, J.E.D.,Zeldin, O.B.,Garman, E.F.,Lea, S.M.,Berks, B.C. (deposition date: 2011-11-29, release date: 2012-12-05, Last modification date: 2023-12-20)

Primary citation

Yong, S.C.,Roversi, P.,Lillington, J.,Rodriguez, F.,Krehenbrink, M.,Zeldin, O.B.,Garman, E.F.,Lea, S.M.,Berks, B.C.
A Complex Iron-Calcium Cofactor Catalyzing Phosphotransfer Chemistry
Science, 345:1170-, 2014

PubMed Abstract: Alkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes, we have determined the structure of the widely occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active-site cofactor comprising two antiferromagnetically coupled ferric iron ions (Fe(3+)), three calcium ions (Ca(2+)), and an oxo group bridging three of the metal ions. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active-site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition.

PubMed: 25190793
DOI: 10.1126/SCIENCE.1254237

Experimental method

X-RAY DIFFRACTION (1.79 Å)