Biomaterial Database

Structure of the Mycobacterium tuberculosis soluble inorganic pyrophosphatase Rv3628 at pH 7.0. 2011

Stefano Benini, and Keith Wilson

Faculty of Science and Technology, Free University of Bolzano, Bolzano, Italy. stefano.benini@unibz.it

The 1.5 Å resolution crystal structure of the Mycobacterium tuberculosis soluble inorganic pyrophosphatase Rv3628 at pH 7.0 is reported. The M. tuberculosis and M. leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site. The role of these two residues in catalysis is not fully understood. Mutational and functional studies of the M. tuberculosis enzyme showed that His21 and His86 are not essential for pyrophosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme. Comparison with the structure previously reported at pH 5.0 provides further insight into the role of the two histidines. Two potassium-binding sites are found as a result of the high potassium concentration in the mother liquor.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D009169	Mycobacterium tuberculosis	A species of gram-positive, aerobic bacteria that produces TUBERCULOSIS in humans, other primates, CATTLE; DOGS; and some other animals which have contact with humans. Growth tends to be in serpentine, cordlike masses in which the bacilli show a parallel orientation.	Mycobacterium tuberculosis H37Rv
D006863	Hydrogen-Ion Concentration	The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH	pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012995	Solubility	The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)	Solubilities
D017434	Protein Structure, Tertiary	The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure.	Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D043564	Inorganic Pyrophosphatase	An enzyme which catalyzes the hydrolysis of diphosphate (DIPHOSPHATES) into inorganic phosphate. The hydrolysis of pyrophosphate is coupled to the transport of HYDROGEN IONS across a membrane.	Pyrophosphatase, Inorganic,H(+)-PPase,H+-Pyrophosphatase,Proton-Pumping Inorganic Pyrophosphatase,Proton-Translocating Pyrophosphatase,Pyrophosphate-Energized Inorganic Pyrophosphatase,H+ Pyrophosphatase,Inorganic Pyrophosphatase, Proton-Pumping,Inorganic Pyrophosphatase, Pyrophosphate-Energized,Proton Pumping Inorganic Pyrophosphatase,Proton Translocating Pyrophosphatase,Pyrophosphatase, Proton-Pumping Inorganic,Pyrophosphatase, Proton-Translocating,Pyrophosphatase, Pyrophosphate-Energized Inorganic,Pyrophosphate Energized Inorganic Pyrophosphatase
D040681	Structural Homology, Protein	The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.	Protein Structural Homology,3-D Homologs, Protein,3-D Homology, Protein,3-Dimensional Homologs, Protein,3-Dimensional Homology, Protein,Homologs, 3-D, Protein,Homologs, 3-Dimensional, Protein,Homologs, Sturctural, Protein,Protein Structural Homologs,Structural Homologs, Protein,3 D Homologs, Protein,3 D Homology, Protein,3 Dimensional Homologs, Protein,3 Dimensional Homology, Protein,3-D Homolog, Protein,3-D Homologies, Protein,3-Dimensional Homolog, Protein,3-Dimensional Homologies, Protein,Homolog, Protein 3-D,Homolog, Protein 3-Dimensional,Homolog, Protein Structural,Homologies, Protein 3-D,Homologies, Protein 3-Dimensional,Homologies, Protein Structural,Homologs, Protein 3-D,Homologs, Protein 3-Dimensional,Homologs, Protein Structural,Homology, Protein 3-D,Homology, Protein 3-Dimensional,Homology, Protein Structural,Protein 3-D Homolog,Protein 3-D Homologies,Protein 3-D Homologs,Protein 3-D Homology,Protein 3-Dimensional Homolog,Protein 3-Dimensional Homologies,Protein 3-Dimensional Homologs,Protein 3-Dimensional Homology,Protein Structural Homolog,Protein Structural Homologies,Structural Homolog, Protein,Structural Homologies, Protein