1HYB

CRYSTAL STRUCTURE OF AN ACTIVE SITE MUTANT OF METHANOBACTERIUM THERMOAUTOTROPHICUM NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE

1HYB の概要

• エントリーDOI: 10.2210/pdb1hyb/pdb
• 関連するPDBエントリー: 1ej2
• 分子名称: NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE, SULFATE ION, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: dinucleotide binding fold, active site mutant, transferase
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20961.01

構造登録者

Saridakis, V.,Christendat, D.,Kimber, M.S.,Edwards, A.M.,Pai, E.F. (登録日: 2001-01-18, 公開日: 2001-03-14, 最終更新日: 2023-08-09)

主引用文献

Saridakis, V.,Christendat, D.,Kimber, M.S.,Dharamsi, A.,Edwards, A.M.,Pai, E.F.
Insights into ligand binding and catalysis of a central step in NAD+ synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes.
J.Biol.Chem., 276:7225-7232, 2001

PubMed Abstract: Nicotinamide mononucleotide adenylyltransferase (NMNATase) catalyzes the linking of NMN(+) or NaMN(+) with ATP, which in all organisms is one of the common step in the synthesis of the ubiquitous coenzyme NAD(+), via both de novo and salvage biosynthetic pathways. The structure of Methanobacterium thermoautotrophicum NMNATase determined using multiwavelength anomalous dispersion phasing revealed a nucleotide-binding fold common to nucleotidyltransferase proteins. An NAD(+) molecule and a sulfate ion were bound in the active site allowing the identification of residues involved in product binding. In addition, the role of the conserved (16)HXGH(19) active site motif in catalysis was probed by mutagenic, enzymatic and crystallographic techniques, including the characterization of an NMN(+)/SO4(2-) complex of mutant H19A NMNATase.

PubMed: 11063748
DOI: 10.1074/jbc.M008810200

実験手法

X-RAY DIFFRACTION (2 Å)