Literature summary for 2.7.7.80 extracted from

Lake, M.; Wuebbens, M.; Rajagopalan, K.; Schindelin, H.
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex (2001), Nature, 414, 325-329.

Crystallization (Commentary)

Crystallization (Comment)	Organism
MoeB-MoaD complex in its apo, ATP-bound, and MoaD-adenylate forms, equal volumes of 23 mg/ml MoeB and 10 mg/ml MoaD at 4°C for 1 h, followed by hanging drop vapour diffusion against a reservoir containing 1.7 M Li2SO4, and 100 mM HEPES, pH 7.5, for the ternary complex, crystals of the apo complex are soaked for 24 h in a solution consisting of 1.7 M Li2SO4, 100 mM HEPES, pH 7.5, and 20 mM ATP, X-ray diffraction structure determination and analysis at 1.7-3.5 A resolutions, modeling	Escherichia coli

Crystallization (Comment)

Organism

MoeB-MoaD complex in its apo, ATP-bound, and MoaD-adenylate forms, equal volumes of 23 mg/ml MoeB and 10 mg/ml MoaD at 4°C for 1 h, followed by hanging drop vapour diffusion against a reservoir containing 1.7 M Li2SO4, and 100 mM HEPES, pH 7.5, for the ternary complex, crystals of the apo complex are soaked for 24 h in a solution consisting of 1.7 M Li2SO4, 100 mM HEPES, pH 7.5, and 20 mM ATP, X-ray diffraction structure determination and analysis at 1.7-3.5 A resolutions, modeling

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D130A	site-directed mutagenesis, inactive mutant	Escherichia coli
D130E	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Escherichia coli
R14A	site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme	Escherichia coli
R14A/R73A	site-directed mutagenesis, inactive mutant	Escherichia coli
R14K	site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme	Escherichia coli
R14K/R73A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Escherichia coli
R73A	site-directed mutagenesis, the mutant shows slighty reduced activity compared to the wild-type enzyme	Escherichia coli
R73K	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly	Escherichia coli	-	diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P12282	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly	-	Escherichia coli	diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP	-	?
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly	-	Escherichia coli	diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP	the Mg2+ may remain associated with the diphosphate-leaving group	?

Subunits

Subunits	Comment	Organism
More	MoeB-MoaD complex formation, the interface is the C-terminal extension of the MoaD C-terminus into a pocket on the MoeB surface, apo- and ligand-bound structures, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
MoeB	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	MoeB beongs to the MoeB/E1 enzyme superfamily, conserved active site structure, overview. The molybdenum cofactor (Moco) biosynthesis, involving Escherichia coli proteins MoeB and MoaD, is an evolutionarily conserved pathway	Escherichia coli
metabolism	Escherichia coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis	Escherichia coli
physiological function	MoeB is involved in molybdenum cofactor (Moco) biosynthesis, it activates the C-terminus of MoaD to form an acyl-adenylate. The MoeB-MoaD interface is the C-terminal extension of the MoaD C-terminus into a pocket on the MoeB surface, MoeB-MoaD-ATP ternary complex structure, overview. A preference for small amino acids (Gly, Ala, Ser) at the centre of beta5 of MoeB, facilitating the insertion of the Gly-Gly motif of MoaD into the active site of MoeB, Arg 14 is inserted into the active site across the dimer interface and has a critical role during ATP hydrolysis	Escherichia coli