Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3

  • Yoshimune K
  • Shirakihara Y
  • Shiratori A
 et al. 
  • 11


    Mendeley users who have this article in their library.
  • 14


    Citations of this article.


Glutaminase of Micrococcus luteus K-3 (intact glutaminase; 48 kDa) is digested to a C-terminally truncated fragment (glutaminase fragment; 42 kDa) that shows higher salt tolerance than that of the intact glutaminase. The crystal structure of the glutaminase fragment was determined at 2.4 Å resolution using multiple-wavelength anomalous dispersion (MAD). The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic serine-lysine dyad (S64 and K67) is located in a cleft of the N-terminal domain. Mutations of the S64 or K67 residues abolished the enzyme activity. The N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism. A diffraction analysis of the intact glutaminase crystals (a twinning fraction of 0.43) located the glutaminase fragment in the unit cell but failed to turn up clear densities for the missing C-terminal portion of the molecule. © 2006 Elsevier Inc. All rights reserved.

Author-supplied keywords

  • Crystal structure
  • Glutaminase
  • Halophilic protein
  • Micrococcus luteus K-3
  • Salt-tolerant glutaminase

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free