Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.4.15 extracted from

  • Gupta, V.; Gupta, R.; Khare, G.; Salunke, D.; Surolia, A.; Tyagi, A.
    Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration (2010), PLoS ONE, 5, e9222.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of dehydrated and hydrated BirA, at 2.69 A and 2.8 A resolution, respectively. Dehydration of BirA crystals traps both the apo and active conformations in its asymmetric unit. The crystal lattice rearrangement due to shrinkage in the dehydrated Mtb-BirA crystals ensues structural order of otherwise flexible ligand-binding loops L4 and L8 in apo BirA. In addition, crystal dehydration results in a shift of 3.5 A in the flexible loop L6, a proline-rich loop unique to Mycobacterium tuberculosis complex as well as around the L11 region. The shift in loop L11 in the C-terminal domain on dehydration emulates the action responsible for the complex formation with its protein ligand biotin carboxyl carrier protein domain of ACCA3. The two subunits A and B, though related by a noncrystallographic twofold symmetry, assemble into an asymmetric dimer representing the ligand-bound and ligand-free states of the protein, respectively Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P96884
-
-

Synonyms

Synonyms Comment Organism
BirA
-
Mycobacterium tuberculosis