1G8L

CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA

Summary for 1G8L

Entry DOI	10.2210/pdb1g8l/pdb
Related	1G8R
Descriptor	MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN, GLYCEROL (3 entities in total)
Functional Keywords	molybdenum cofactor biosynthesis, metal binding protein
Biological source	Escherichia coli
Total number of polymer chains	2
Total formula weight	89869.81
Authors	Xiang, S.,Nichols, J.,Rajagopalan, K.V.,Schindelin, H. (deposition date: 2000-11-17, release date: 2001-05-02, Last modification date: 2024-02-07)
Primary citation	Xiang, S.,Nichols, J.,Rajagopalan, K.V.,Schindelin, H. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure, 9:299-310, 2001 Cited by PubMed Abstract: Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in archaea, eubacteria, and eukaryotes. In humans, genetic abnormalities in the biosynthetic pathway result in Moco deficiency, which is accompanied by severe neurological symptoms and death shortly after birth. The Escherichia coli MoeA and MogA proteins are involved in the final step of Moco biosynthesis: the incorporation of molybdenum into molybdopterin (MPT), the organic pyranopterin moiety of Moco. PubMed: 11525167 DOI: 10.1016/S0969-2126(01)00588-3 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation