The refined structure of beef liver catalase at 2·5 Å resolution

Fita, Ignacio; Silva, A.M.; Murthy, M.R.N.; Rossmann, M.G.

doi:10.1107/s0108768186097835

Cited by 107 publications

(59 citation statements)

References 9 publications

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“…BLC tightly binds NADPH [3]. In the equivalent position in the electron density map of MLC at 3 A resolution there ::'as some electron density which allowed us to suppose that MLC also binds NADPH [7,8].…”

Section: Resultsmentioning

confidence: 99%

“…To date~ the three-dimensional structures of two eatalases have been determined and refined: beef liver catalase (BLC) at 2.5 A resolution [3] and that of the fungus, Penicillium t,itale (PVC), at 2.0 A resolution [4,5]. Previously we have investigated the polypeptide chain folding in two bacterial catalases, the non-harm hexameric Mn-catalase from Thermus tt,.ermophilus with a different subunit organization [6], and the tetra- deikticus (MLC) with spatial organization closely resembling that of BLC [7,8].…”

Section: Introductionmentioning

confidence: 99%

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Three‐dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution

et al. 1992

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The three-dimensional crystal structure of~_atalase from Micrococa~s lysodeikticus has been solved by multiple isomorphous replacement and refined at 1.5 A resolution. The subunit of the tetramerlc molectde of 222 symmetry consists of a single polypeptide chain of about 500 amino acid residues and one harm group. The crystals Ixlong to space group P422~2 with unit cell parameters a = b = 106.7 A, c = 106.3 A. and there is one subunit of the tetramer per asymmetric unit. The amino acid sequence has been tentatively determined by computer graphics model building and comparison with the known three-dimensional structure of beef liver camlase and sequences ol'seveml other catalases. The atomic mcn:lel has been refined by Hendriekson and Konnert's least-squares minimisation against 94,315 reflections between 8 A and 1.5 A. The final model consists of 3,977 non-h::drogen atoms of the protein and haem group, 426 water molecules and one sulphate ion. The secondaIT and tertiary structures of the bacterial catalase have been analyzed and a comparison with the structure of b~f liver catalase has been made.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Three‐dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution

et al. 1992

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“…The structure of a 3-methyl salicylic acidiron complex [16] was taken from the Cambridge Structural Database (Refcode JETTEH) and the iron atom superimposed on the iron atom of bovine catalase (PDB access code 8CAT) [17]. SA fits well into the catalytic cleft of the protein with only a single steric clash (Ile-164, see below) that may not be relieved by minor torsions around rotable bonds.…”

Section: Riiffer Et Al/febs Letters 377 (1995) 175-180mentioning

confidence: 99%

Evidence against specific binding of salicylic acid to plant catalase

1995

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It was demonstrated that salicylic acid (SA) not only binds to catalase from differentiated higher plants and plant cell suspension cultures but also to those of fungi and animals. SA bound specifically to iron-containing enzymes, such as catalase, aconitase, lipoxidase and peroxidase, while not to iron-free plant enzymes. On the grounds of these experiments, the claim is further challenged that SA is a signalling compound and second messenger in plants that activates plant defense-related genes through elevated H202 levels by specifically inhibiting catalase activity. SA may just function as a phytoalexin.

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“…The structures of six catalases have now been solved including those from bovine liver~BLC!~Murthy et Fita et al, 1986!, Penicillium vitale~PVC!~Vainshtein et al, 1981!, Proteus mirabilis~PMC!~Gouet et al, 1995!, Micrococcus lysodeikticus~MLC!~Murshudov et al, 1992!, Saccharomyces cerevisiae~SCCA!~Berthet et al, 1997Maté et al, 1999!, andEscherichia coli~HPII!~Bravo et al, 1995;Bravo et al, 1998! revealing a common highly conserved core in all enzymes.…”

mentioning

confidence: 99%

Role of the lateral channel in catalase HPII of Escherichia coli

et al. 1999

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The heme-containing catalase HPII of Escherichia coli consists of a homotetramer in which each subunit contains a core region with the highly conserved catalase tertiary structure, to which are appended N-and C-terminal extensions making it the largest known catalase. HPII does not bind NADPH, a cofactor often found in catalases. In HPII, residues 585-590 of the C-terminal extension protrude into the pocket corresponding to the NADPH binding site in the bovine liver catalase. Despite this difference, residues that define the NADPH pocket in the bovine enzyme appear to be well preserved in HPII. Only two residues that interact ionically with NADPH in the bovine enzyme~Asp212 and His304! differ in HPII~Glu270 and Glu362!, but their mutation to the bovine sequence did not promote nucleotide binding. The active-site heme groups are deeply buried inside the molecular structure requiring the movement of substrate and products through long channels. One potential channel is about 30 Å in length, approaches the heme active site laterally, and is structurally related to the branched channel associated with the NADPH binding pocket in catalases that bind the dinucleotide. In HPII, the upper branch of this channel is interrupted by the presence of Arg260 ionically bound to Glu270. When Arg260 is replaced by alanine, there is a threefold increase in the catalytic activity of the enzyme. Inhibitors of HPII, including azide, cyanide, various sulfhydryl reagents, and alkylhydroxylamine derivatives, are effective at lower concentration on the Ala260 mutant enzyme compared to the wild-type enzyme. The crystal structure of the Ala260 mutant variant of HPII, determined at 2.3 Å resolution, revealed a number of local structural changes resulting in the opening of a second branch in the lateral channel, which appears to be used by inhibitors for access to the active site, either as an inlet channel for substrate or an exhaust channel for reaction products.

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The refined structure of beef liver catalase at 2·5 Å resolution

Cited by 107 publications

References 9 publications

Three‐dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution

Three‐dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution

Evidence against specific binding of salicylic acid to plant catalase

Role of the lateral channel in catalase HPII of Escherichia coli

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