title: PASTA in Penicillin Binding Proteins and Serine/Threonine Kinases: A Recipe of Structural, Dynamic and Binding Properties.
abstract: BACKGROUND
  Penicillin binding proteins (PBPs) and Serine Threonine kinases (STPKs) are two classes of bacterial enzymes whose involvement in a series of vital processes in bacterial growth and division is well assessed. Many PBPs and STPKs show linked an ancillary domain named PASTA, whose functional role is not completely deciphered so far. It has been proposed that PASTAs are sensor modules that by binding opportune ligands (i.e. muropeptides) activate the cognate proteins to their functions. However, based on recent data, the sensor annotation sounds true for PASTA from STPKs, and false for PASTA from PBPs.
  
  
  OBJECTIVE
  Different PASTA domains, belonging or not to different protein classes, sharing or not appreciable sequence identities, always show identical folds. This survey of the structural, binding and dynamic properties of PASTA domains pursues the reasons why identical topologies may turn in different roles.
  
  
  RESULTS
  Amino acid compositions, total charges and distribution of the hydrophobic/hydrophilic patches on the surface, significantly vary among PASTAs from STPKs and PBPs and appear to correlate with different functions. A possible criterion to discriminate between PASTA modules of STPKs or PBPs solely based on their sequences is proposed. Possibly reflecting different species as well as functional roles and evolutionary profile, our routine represents a fast even though approximate method to distinguish between PASTA belonging to different classes.
authors.affiliation: CIRPeB, University of Naples Federico II, via Mezzocannone 16, 80134, Naples, Italy.
authors.forename: Luisa
authors.initials: L
authors.lastname: Calvanese
authors.affiliation: CIRPeB, University of Naples Federico II, via Mezzocannone 16, 80134, Naples, Italy.|Department of Pharmacy, University of Naples "Federico II", via Mezzocannone 16, 80134, Naples, Italy.|Institute of Biostructures and Bio-imaging- CNR, via Mezzocannone, 16, 80134, Naples, Italy.
authors.forename: Lucia
authors.initials: L
authors.lastname: Falcigno
authors.affiliation: Institute of Biostructures and Bio-imaging- CNR, via Mezzocannone, 16, 80134, Naples, Italy.
authors.forename: Flavia
authors.initials: F
authors.lastname: Squeglia
authors.affiliation: CIRPeB, University of Naples Federico II, via Mezzocannone 16, 80134, Naples, Italy.|Department of Pharmacy, University of Naples "Federico II", via Mezzocannone 16, 80134, Naples, Italy.|Institute of Biostructures and Bio-imaging- CNR, via Mezzocannone, 16, 80134, Naples, Italy.
authors.forename: Gabriella
authors.initials: G
authors.lastname: D'Auria
authors.affiliation: Institute of Biostructures and Bio-imaging- CNR, via Mezzocannone, 16, 80134, Naples, Italy.
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
mesh_terms: D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D030562:Databases, Protein; D046915:Penicillin-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D000072417:Protein Domains; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D046915:Penicillin-Binding Proteins; D017346:Protein Serine-Threonine Kinases
keywords: PASTA domain; PBPs.; dynamics; fold; functional annotation; protein structure; sequence