1E5K

CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA (PROTEIN FA) FROM ESCHERICHIA COLI AT NEAR ATOMIC RESOLUTION

Summary for 1E5K

Entry DOI	10.2210/pdb1e5k/pdb
Descriptor	MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS PROTEIN A, LITHIUM ION, CITRIC ACID, ... (4 entities in total)
Functional Keywords	molybdopterin nucleotidyl-transferase
Biological source	ESCHERICHIA COLI
Total number of polymer chains	1
Total formula weight	22977.00
Authors	Stevenson, C.E.M.,Sargent, F.,Buchanan, G.,Palmer, T.,Lawson, D.M. (deposition date: 2000-07-27, release date: 2000-11-07, Last modification date: 2024-05-08)
Primary citation	Stevenson, C.E.M.,Sargent, F.,Buchanan, G.,Palmer, T.,Lawson, D.M. Crystal Structure of the Molybdenum Cofactor Biosynthesis Protein Moba from Escherichia Coli at Near Atomic Resolution Structure, 8:1115-, 2000 Cited by PubMed Abstract: All mononuclear molybdoenzymes bind molybdenum in a complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This modification reaction is required for the functioning of many bacterial molybdoenzymes, including the nitrate reductases, dimethylsulfoxide (DMSO) and trimethylamine-N-oxide (TMAO) reductases, and formate dehydrogenases. The GMP attachment step is catalyzed by the cellular enzyme MobA. PubMed: 11080634 DOI: 10.1016/S0969-2126(00)00518-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.35 Å)

Structure validation