2dfw

From Proteopedia

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

Overview

Glutaminase of Micrococcus luteus K-3 (intact glutaminase; 48kDa) is digested to a C-terminally truncated fragment (glutaminase fragment; 42kDa) that shows higher salt tolerance than that of the intact glutaminase. The crystal structure of the glutaminase fragment was determined at 2.4A 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.

About this Structure

2DFW is a Single protein structure of sequence from Micrococcus luteus. Active as Glutaminase, with EC number 3.5.1.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3., Yoshimune K, Shirakihara Y, Shiratori A, Wakayama M, Chantawannakul P, Moriguchi M, Biochem Biophys Res Commun. 2006 Aug 11;346(4):1118-24. Epub 2006 Jun 6. PMID:16793004

Page seeded by OCA on Thu Feb 21 16:58:21 2008