Structure of the Native MoeB-MoaD Protein Complex

Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.

MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1

MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN D

MAELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLASAGVGNLTLLDFDTVSLSNLQRQTLHSDA
TVGQPKVESARDALTRINPHIAITPVNALLDDAELAALIAEHDLVLDCTDNVAVRNQLNAGCFAAKVPLVSGAAIRMEGQ
ITVFTYQDGEPCYRCLSRLFGENALTCVEAGVMAPLIGVIGSLQAMEAIKMLAGYGKPASGKIVMYDAMTCQFREMKLMR
NPGCEVCGQ

MIKVLFFAQVRELVGTDATEVAADFPTVEALRQHMAAQSDRWALALEDGKLLAAVNQTLVSFDHPLTDGDEVAFFPPVTG
G

Lithium Sulfate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Structure of Molybdopterin Synthase (MoaD in complex with MoaE)

Structure of the ATP-bound MoeB-MoaD protein complex

Structure of the Covalent Acyl-Adenylate Form of the MoeB-MoaD Protein Complex

The asymmetric unit contains a heterodimer comprised of (1) molecule of MoeB and (1) molecule of MoaD. The heterotetramer is generated by applying: -y+1,-x+1,1/2-z

MoeB: modified Rossmann fold; (2) Cys-X-X-Cys Zinc-binding motifs; MoaD: ubiquitin-like fold, LIGASE