1M7S

Crystal Structure Analysis of Catalase CatF of Pseudomonas syringae

1M7S の概要

• エントリーDOI: 10.2210/pdb1m7s/pdb
• 分子名称: Catalase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: beta barrel, alpha helical domain, oxidoreductase
• 由来する生物種: Pseudomonas syringae
• 細胞内の位置: Periplasm (Probable): P46206
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 218635.17

構造登録者

Carpena, X.,Soriano, M.,Klotz, M.G.,Duckworth, H.W.,Donald, L.J.,Melik-Adamyan, W.,Fita, I.,Loewen, P.C. (登録日: 2002-07-22, 公開日: 2002-08-28, 最終更新日: 2024-02-14)

主引用文献

Carpena, X.,Soriano, M.,Klotz, M.G.,Duckworth, H.W.,Donald, L.J.,Melik-Adamyan, W.,Fita, I.,Loewen, P.C.
Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution
Proteins, 50:423-436, 2003

PubMed Abstract: Catalase CatF of Pseudomonas syringae has been identified phylogenetically as a clade 1 catalase, closely related to plant catalases, a group from which no structure has been determined. The structure of CatF has been refined at 1.8 A resolution by using X-ray synchrotron data collected from a crystal flash-cooled with liquid nitrogen. The crystallographic agreement factors R and R(free) are, respectively, 18.3% and 24.0%. The asymmetric unit of the crystal contains a whole molecule that shows accurate 222-point group symmetry. The crystallized enzyme is a homotetramer of subunits with 484 residues, some 26 residues shorter than predicted from the DNA sequence. Mass spectrometry analysis confirmed the absence of 26 N-terminal residues, possibly removed by a periplasmic transport system. The core structure of the CatF subunit was closely related to seven other catalases with root-mean-square deviations (RMSDs) of 368 core Calpha atoms of 0.99-1.30 A. The heme component of CatF is heme b in the same orientation that is found in Escherichia coli hydroperoxidase II, an orientation that is flipped 180 degrees with respect the orientation of the heme in bovine liver catalase. NADPH is not found in the structure of CatF because key residues required for nucleotide binding are missing; 2129 water molecules were refined into the model. Water occupancy in the main or perpendicular channel of CatF varied among the four subunits from two to five in the region between the heme and the conserved Asp150. A comparison of the water occupancy in this region with the same region in other catalases reveals significant differences among the catalases.

PubMed: 12557185
DOI: 10.1002/prot.10284

実験手法

X-RAY DIFFRACTION (1.8 Å)