2ASF

Crystal structure of the conserved hypothetical protein Rv2074 from Mycobacterium tuberculosis 1.6 A

2ASF の概要

• エントリーDOI: 10.2210/pdb2asf/pdb
• 関連するPDBエントリー: 1xxo
• 分子名称: Hypothetical protein Rv2074, SODIUM ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: rv2074, h37rv, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15514.01

構造登録者

Biswal, B.K.,Au, K.,Cherney, M.M.,Garen, C.,James, M.N.,TB Structural Genomics Consortium (TBSGC) (登録日: 2005-08-23, 公開日: 2005-10-11, 最終更新日: 2024-10-23)

主引用文献

Biswal, B.K.,Au, K.,Cherney, M.M.,Garen, C.,James, M.N.
The molecular structure of Rv2074, a probable pyridoxine 5'-phosphate oxidase from Mycobacterium tuberculosis, at 1.6 angstroms resolution.
Acta Crystallogr.,Sect.F, 62:735-742, 2006

PubMed Abstract: The crystal structure of a conserved hypothetical protein corresponding to open reading frame Rv2074 from Mycobacterium tuberculosis (Mtb) has been solved by the two-wavelength anomalous dispersion method. Refinement of the molecular structure at 1.6 angstroms resolution resulted in an R(work) of 0.178 and an R(free) of 0.204. The crystal asymmetric unit contains an Rv2074 monomer; however, the crystallographic twofold symmetry operation of space group P4(3)2(1)2 generates dimeric Rv2074. Each monomer folds into a six-stranded antiparallel beta-barrel flanked by two alpha-helices. The three-dimensional structure of Rv2074 is very similar to that of Mtb Rv1155, a probable pyridoxine 5'-phosphate oxidase (PNPOx), which corroborates well with the relatively high sequence similarity (52%) between the two. A structural comparison between Rv2074 and Rv1155 revealed that the core structure (a six-stranded beta-barrel) is also well conserved; the major differences between the two lie in the N- and C-termini and in the small helical domain. Two citric acid molecules were observed in the active site of Rv2074, the crystals of which were grown in 0.2 M sodium citrate buffer pH 5.0. The citric acid molecules are bound to Rv2074 by hydrogen-bonding interactions with Thr55, Gln60 and Lys61. One of the two citric acid molecules occupies the same spatial position that corresponds to the position of the phosphate and ribose sugar moieties of the flavin mononucleotide (FMN) in the Mtb Rv1155-FMN, Escherichia coli PNPOx-FMN and human PNPOx-FMN complex structures. Owing to its extensive structural similarity with Mtb Rv1155 and to the E. coli and human PNPOx enzymes, Rv2074 may be involved in the final step in the biosynthesis of pyridoxal 5'-phosphate (PLP; a vitamin B6).

PubMed: 16880544
DOI: 10.1107/S1744309106025012

実験手法

X-RAY DIFFRACTION (1.6 Å)