1N7G

Crystal Structure of the GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP-rhamnose.

1N7G の概要

• エントリーDOI: 10.2210/pdb1n7g/pdb
• 分子名称: GDP-D-mannose-4,6-dehydratase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GUANOSINE-5'-DIPHOSPHATE-RHAMNOSE, ... (4 entities in total)
• 機能のキーワード: rossmann fold, sdr, short-chain dehydrogenase/reductase, lyase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 177086.93

構造登録者

Mulichak, A.M.,Bonin, C.P.,Reiter, W.-D.,Garavito, R.M. (登録日: 2002-11-14, 公開日: 2003-01-07, 最終更新日: 2024-02-14)

主引用文献

Mulichak, A.M.,Bonin, C.P.,Reiter, W.-D.,Garavito, R.M.
The structure of the MUR1 GDP-mannose 4,6-dehydratase from A. thaliana: Implications for ligand binding and specificity.
Biochemistry, 41:155578-155589, 2002

PubMed Abstract: GDP-D-mannose 4,6-dehydratase catalyzes the first step in the de novo synthesis of GDP-L-fucose, the activated form of L-fucose, which is a component of glycoconjugates in plants known to be important to the development and strength of stem tissues. We have determined the three-dimensional structure of the MUR1 dehydratase isoform from Arabidopsis thaliana complexed with its NADPH cofactor as well as with the ligands GDP and GDP-D-rhamnose. MUR1 is a member of the nucleoside-diphosphosugar modifying subclass of the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr, and Ser/Thr residues. MUR1 is the first member of this subfamily to be observed as a tetramer, the interface of which reveals a close and intimate overlap of neighboring NADP(+)-binding sites. The GDP moiety of the substrate also binds in an unusual syn conformation. The protein-ligand interactions around the hexose moiety of the substrate support the importance of the conserved triad residues and an additional Glu side chain serving as a general base for catalysis. Phe and Arg side chains close to the hexose ring may serve to confer substrate specificity at the O2 position. In the MUR1/GDP-D-rhamnose complex, a single unique monomer within the protein tetramer that has an unoccupied substrate site highlights the conformational changes that accompany substrate binding and may suggest the existence of negative cooperativity in MUR1 function.

PubMed: 12501186
DOI: 10.1021/bi0266683

実験手法

X-RAY DIFFRACTION (2.2 Å)