Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution. Academic Article

abstract

• The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 A resolution. PPC synthetase is a dimer with identical monomers. Some features of the monomer fold resemble a group of NAD-dependent enzymes, while other features resemble the ribokinase fold. The ATP, phosphopantothenate, and cysteine binding sites were deduced from modeling studies. Highly conserved ATP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, Ala180, and Asp183 from one monomer and Arg55' from the adjacent monomer. The structure predicts a ping pong mechanism with initial formation of an acyladenylate intermediate, followed by release of pyrophosphate and attack by cysteine to form the final products PPC and AMP.

authors

• Begley, Tadhg

published proceedings

• Structure

altmetric score

• 3

author list (cited authors)

• Manoj, N., Strauss, E., Begley, T. P., & Ealick, S. E.

citation count

• 27

complete list of authors

• Manoj, Narayanan||Strauss, Erick||Begley, Tadhg P||Ealick, Steven E

publication date

• August 2003

publisher

• Elsevier  Publisher

published in

• Structure  Journal

keywords

• Amino Acid Sequence
• Binding Sites
• Cell Transformation, Viral
• Conserved Sequence
• Crystallography, X-Ray
• Dimerization
• Escherichia Coli
• Genetic Vectors
• Humans
• Models, Molecular
• Molecular Sequence Data
• Molecular Structure
• Peptide Synthases
• Phosphotransferases (Alcohol Group Acceptor)
• Protein Binding
• Protein Structure, Secondary
• Protein Structure, Tertiary
• Sequence Homology, Amino Acid
• Spectrum Analysis, Raman
• Substrate Specificity
• Tobacco Mosaic Virus

Digital Object Identifier (DOI)

• 10.1016/s0969-2126(03)00146-1

start page

• 927

end page

• 936

volume

• 11

issue

• 8

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fs0969-2126%2803%2900146-1