4CAT

THREE-DIMENSIONAL STRUCTURE OF CATALASE FROM PENICILLIUM VITALE AT 2.0 ANGSTROMS RESOLUTION

Summary for 4CAT

• Entry DOI: 10.2210/pdb4cat/pdb
• Descriptor: CATALASE, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• Functional Keywords: oxidoreductase(h2o2(a))
• Biological source: Penicillium janthinellum
• Total number of polymer chains: 2
• Total formula weight: 113437.46

Authors

Vainshtein, B.K.,Melik-Adamyan, W.R.,Barynin, V.V.,Vagin, A.A.,Grebenko, A.I. (deposition date: 1983-02-24, release date: 1983-09-06, Last modification date: 2023-09-27)

Primary citation

Vainshtein, B.K.,Melik-Adamyan, W.R.,Barynin, V.V.,Vagin, A.A.,Grebenko, A.I.,Borisov, V.V.,Bartels, K.S.,Fita, I.,Rossmann, M.G.
Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution.
J.Mol.Biol., 188:49-61, 1986

PubMed Abstract: The three-dimensional structure analysis of crystalline fungal catalase from Penicillium vitale has been extended to 2.0 A resolution. The crystals belong to space group P3(1)21, with the unit cell parameters of a = b = 144.4 A and c = 133.8 A. The asymmetric unit contains half a tetrameric molecule of 222 symmetry. Each subunit is a single polypeptide chain of approximately 670 amino acid residues and binds one heme group. The amino acid sequence has been tentatively determined by computer graphics model building (using the FRODO system) and comparison with the known sequence of beef liver catalase. The atomic model has been refined by the Hendrickson & Konnert (1981) restrained least-squares program against 68,000 reflections between 5 A and 2 A resolution. The final R-factor is 0.31 after 24 refinement cycles. The secondary and tertiary structure of the catalase has been analyzed.

PubMed: 3712443
DOI: 10.1016/0022-2836(86)90479-1

Experimental method

X-RAY DIFFRACTION (3 Å)