Abstract
The last enzyme in the arginine-biosynthesis pathway, argininosuccinate lyase, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized, and preliminary X-ray studies have been carried out on the crystals. The His-tagged tetrameric enzyme with a subunit molecular weight of 50.9 kDa crystallized with two tetramers in the asymmetric unit of the orthorhombic unit cell, space group P2(1)2(1)2(1). Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule.
Keywords:
Mycobacterium tuberculosis; Rv1659; argininosuccinate lyase.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Argininosuccinate Lyase / chemistry*
-
Argininosuccinate Lyase / genetics
-
Argininosuccinate Lyase / metabolism
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism
-
Cloning, Molecular
-
Crystallization
-
Crystallography, X-Ray
-
Escherichia coli / genetics
-
Escherichia coli / metabolism
-
Gene Expression
-
Histidine / chemistry
-
Histidine / genetics
-
Mycobacterium tuberculosis / chemistry*
-
Mycobacterium tuberculosis / enzymology
-
Mycobacterium tuberculosis / genetics
-
Oligopeptides / chemistry
-
Oligopeptides / genetics
-
Protein Multimerization
-
Protein Subunits / chemistry*
-
Protein Subunits / genetics
-
Protein Subunits / metabolism
-
Recombinant Fusion Proteins / chemistry
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
Substances
-
Bacterial Proteins
-
His-His-His-His-His-His
-
Oligopeptides
-
Protein Subunits
-
Recombinant Fusion Proteins
-
Histidine
-
Argininosuccinate Lyase