1H4C

Biochemical and Structural Analysis of the Molybdenum Cofactor Biosynthesis protein MobA

1H4C の概要

• エントリーDOI: 10.2210/pdb1h4c/pdb
• 関連するPDBエントリー: 1E5K 1FR9 1FRW 1H4D 1H4E 1HJJ 1HJL
• 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, molybdenum cofactor biosynthesis, gtp-binding
• 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: 22890.89

構造登録者

Guse, A.,Stevenson, C.E.M.,Kuper, J.,Buchanan, G.,Schwarz, G.,Mendel, R.R.,Lawson, D.M.,Palmer, T. (登録日: 2003-02-26, 公開日: 2003-05-08, 最終更新日: 2023-12-13)

主引用文献

Guse, A.,Stevenson, C.E.M.,Kuper, J.,Buchanan, G.,Schwarz, G.,Giordano, G.,Magalon, A.,Mendel, R.R.,Lawson, D.M.,Palmer, T.
Biochemical and Structural Analysis of the Molybdenum Cofactor Biosynthesis Protein Moba
J.Biol.Chem., 278:25302-, 2003

PubMed Abstract: Molybdopterin guanine dinucleotide (MGD) is the form of the molybdenum cofactor that is required for the activity of most bacterial molybdoenzymes. MGD is synthesized from molybdopterin (MPT) and GTP in a reaction catalyzed by the MobA protein. Here we report that wild type MobA can be copurified along with bound MPT and MGD, demonstrating a tight binding of both its substrate and product. To study structure-function relationships, we have constructed a number of site-specific mutations of the most highly conserved amino acid residues of the MobA protein family. Variant MobA proteins were characterized for their ability to support the synthesis of active molybdenum enzymes, to bind MPT and MGD, to interact with the molybdenum cofactor biosynthesis proteins MobB and MoeA. They were also characterized by x-ray structural analysis. Our results suggest an essential role for glycine 15 of MobA, either for GTP binding and/or catalysis, and an involvement of glycine 82 in the stabilization of the product-bound form of the enzyme. Surprisingly, the individual and double substitution of asparagines 180 and 182 to aspartate did not affect MPT binding, catalysis, and product stabilization.

PubMed: 12719427
DOI: 10.1074/JBC.M302639200

実験手法

X-RAY DIFFRACTION (1.65 Å)