2EWS

Crystal structure of S.aureus pantothenate kinase

Summary for 2EWS

• Entry DOI: 10.2210/pdb2ews/pdb
• Descriptor: Pantothenate kinase, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: pank, structural genomics, structural genomics consortium, sgc, transferase
• Biological source: Staphylococcus aureus subsp. aureus
• Total number of polymer chains: 2
• Total formula weight: 63657.60

Authors

Hong, B.S.,Park, H.W.,Structural Genomics Consortium (SGC) (deposition date: 2005-11-06, release date: 2006-09-12, Last modification date: 2024-02-14)

Primary citation

Hong, B.S.,Yun, M.K.,Zhang, Y.M.,Chohnan, S.,Rock, C.O.,White, S.W.,Jackowski, S.,Park, H.W.,Leonardi, R.
Prokaryotic Type II and Type III Pantothenate Kinases: The Same Monomer Fold Creates Dimers with Distinct Catalytic Properties.
Structure, 14:1251-1261, 2006

PubMed Abstract: Three distinct isoforms of pantothenate kinase (CoaA) in bacteria catalyze the first step in coenzyme A biosynthesis. The structures of the type II (Staphylococcus aureus, SaCoaA) and type III (Pseudomonas aeruginosa, PaCoaA) enzymes reveal that they assemble nearly identical subunits with actin-like folds into dimers that exhibit distinct biochemical properties. PaCoaA has a fully enclosed pantothenate binding pocket and requires a monovalent cation to weakly bind ATP in an open cavity that does not interact with the adenine nucleotide. Pantothenate binds to an open pocket in SaCoaA that strongly binds ATP by using a classical P loop architecture coupled with specific interactions with the adenine moiety. The PaCoaA*Pan binary complex explains the resistance of bacteria possessing this isoform to the pantothenamide antibiotics, and the similarity between SaCoaA and human pantothenate kinase 2 explains the molecular basis for the development of the neurodegenerative phenotype in three mutations in the human protein.

PubMed: 16905099
DOI: 10.1016/j.str.2006.06.008

Experimental method

X-RAY DIFFRACTION (2.05 Å)