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

BRENDA support

Literature summary for 2.8.1.12 extracted from

  • Wang, H.; Chen, X.; Zhang, W.; Zhou, W.; Liu, X.; Rao, Z.
    Structural analysis of molybdopterin synthases from two mycobacterial pathogens (2019), Biochem. Biophys. Res. Commun., 511, 21-27 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 2.1 A resolution. The overall structure is hetero-tetrameric, consisting of a MoaE2 dimer flanked on either side by single MoaD2 subunits. The carboxyl-terminal domain of MoaD2 inserted into MoaE2, forming the active pocket Mycobacterium tuberculosis
structure at 2.6 A resolution. The overall structure is hetero-tetrameric, consisting of a MoaE2 dimer flanked on either side by single MoaD2 subunits. The carboxyl-terminal domain of MoaD2 inserted into MoaE2, forming the active pocket Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A0A045HUW8
-
-
Mycolicibacterium smegmatis I7FL16
-
-
Mycolicibacterium smegmatis ATCC 700084 I7FL16
-
-

Synonyms

Synonyms Comment Organism
MoaE2
-
Mycobacterium tuberculosis
MoaE2
-
Mycolicibacterium smegmatis
molybdenum cofactor biosynthesis protein
-
Mycolicibacterium smegmatis
molybdenum cofactor biosynthesis protein E
-
Mycobacterium tuberculosis