1E5K

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

1E5K の概要

• エントリーDOI: 10.2210/pdb1e5k/pdb
• 分子名称: MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS PROTEIN A, LITHIUM ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: molybdopterin nucleotidyl-transferase
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22977.00

構造登録者

Stevenson, C.E.M.,Sargent, F.,Buchanan, G.,Palmer, T.,Lawson, D.M. (登録日: 2000-07-27, 公開日: 2000-11-07, 最終更新日: 2024-05-08)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.35 Å)