Ontology highlight
ABSTRACT:
SUBMITTER: Luo HB
PROVIDER: S-EPMC2830209 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Luo Hai-Bin HB Zheng Heping H Zimmerman Matthew D MD Chruszcz Maksymilian M Skarina Tatiana T Egorova Olga O Savchenko Alexei A Edwards Aled M AM Minor Wladek W
Journal of structural biology 20091120 3
A crystal structure of the putative N-carbamoylsarcosine amidase (CSHase) Ta0454 from Thermoplasma acidophilum was solved by single-wavelength anomalous diffraction and refined at a resolution of 2.35A. CSHases are involved in the degradation of creatinine. Ta0454 shares a similar fold and a highly conserved C-D-K catalytic triad (Cys123, Asp9, and Lys90) with the structures of three cysteine hydrolases (PDB codes 1NBA, 1IM5, and 2H0R). Molecular dynamics (MD) simulations of Ta0454/N-carbamoylsa ...[more]