1R0L

1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH

1R0L の概要

• エントリーDOI: 10.2210/pdb1r0l/pdb
• 関連するPDBエントリー: 1R0K
• 分子名称: 1-deoxy-D-xylulose 5-phosphate reductoisomerase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: reductoisomerase, nadph complex, fosmidomycin, non-mevalonate pathway, zymomonas mobilis, oxidoreductase
• 由来する生物種: Zymomonas mobilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 170541.75

構造登録者

Ricagno, S.,Grolle, S.,Bringer-Meyer, S.,Sahm, H.,Lindqvist, Y.,Schneider, G. (登録日: 2003-09-22, 公開日: 2004-07-13, 最終更新日: 2023-08-23)

主引用文献

Ricagno, S.,Grolle, S.,Bringer-Meyer, S.,Sahm, H.,Lindqvist, Y.,Schneider, G.
Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase from Zymomonas mobilis at 1.9-A resolution.
Biochim.Biophys.Acta, 1698:37-44, 2004

PubMed Abstract: 1-Deoxy-d-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A resolution, and that of a binary complex with the co-substrate NADPH to 2.7-A resolution. The subunit of DXR consists of three domains. Residues 1-150 form the NADPH binding domain, which is a variant of the typical dinucleotide-binding fold. The second domain comprises a four-stranded mixed beta-sheet, with three helices flanking the sheet. Most of the putative active site residues are located on this domain. The C-terminal domain (residues 300-386) folds into a four-helix bundle. In solution and in the crystal, the enzyme forms a homo-dimer. The interface between the two monomers is formed predominantly by extension of the sheet in the second domain. The adenosine phosphate moiety of NADPH binds to the nucleotide-binding fold in the canonical way. The adenine ring interacts with the loop after beta1 and with the loops between alpha2 and beta2 and alpha5 and beta5. The nicotinamide ring is disordered in crystals of this binary complex. Comparisons to Escherichia coli DXR show that the two enzymes are very similar in structure, and that the active site architecture is highly conserved. However, there are differences in the recognition of the adenine ring of NADPH in the two enzymes.

PubMed: 15063313
DOI: 10.1016/j.bbapap.2003.10.006

実験手法

X-RAY DIFFRACTION (2.7 Å)