Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases

Proteins. 2007 Nov 1;69(2):415-21. doi: 10.1002/prot.21314.
No abstract available

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology
  • Binding Sites
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Neisseria meningitidis / enzymology*
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphoric Monoester Hydrolases / physiology
  • Protein Structure, Secondary

Substances

  • Bacterial Proteins
  • Phosphoric Monoester Hydrolases

Associated data

  • PDB/2F46