The Structure of Rigidoporus lignosus Laccase Containing a Full Complement of Copper Ions, Reveals an Asymmetrical Arrangement for the T3 Copper Pair

Garavaglia, Silvia; Cambria, Maria Teresa; Miglio, Marco; Ragusa, Santa; Iacobazzi, Vito; Palmieri, Ferdinando; D’Ambrosio, Chiara; Scaloni, Andrea; Rizzi, Menico

doi:10.1016/j.jmb.2004.07.100

Cited by 148 publications

(94 citation statements)

References 51 publications

(81 reference statements)

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“…These structural asymmetries were also reported in other laccases (Ferraroni et al, 2007;Garavaglia et al, 2004;Lyashenko et al, 2006;Matera et al, 2008). Theoretical calculations on ascorbate oxidase revealed that the Cu1-Cu3a pathway was up to three times more efficient than the Cu1-Cu3b in electron transfer (Kyritsis et al, 1993).…”

Section: Trinuclear Centersupporting

confidence: 68%

Structural insight into the oxidation of sinapic acid by CotA laccase

Xie

Liu

et al. 2015

Journal of Structural Biology

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Section: Trinuclear Centersupporting

confidence: 68%

Structural insight into the oxidation of sinapic acid by CotA laccase

Xie

Liu

et al. 2015

Journal of Structural Biology

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“…The T1 sites in domains 4 and 6 are typical blue-copper sites with two histidines and a cysteine ligand at around 2.0 Å and a fourth weaker ligand, a methionine, at distance of around 3.0 Å (Table 3). The mononuclear site in domain 2 is similar to that found in several fungal laccases (Ducros et al, 2001;Piontek et al, 2002;Garavaglia et al, 2004) in that it lacks the weak methionine ligand, which is replaced by an aliphatic leucine residue at a closest distance of around 3.5 Å . These three sites are not significantly different from those described in detail for the room-temperature structure.…”

Section: The Mononuclear T1 Copper-binding Sitesmentioning

confidence: 56%

Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites

Bento

Peixoto

Zaĭtsev

et al. 2007

Acta Crystallogr D Biol Crystallogr

123

108

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“…The T1 sites are located in domain 1 of each subunit and are ϳ13 Å from the nearest T2/T3 cluster. Although access to the BCO T1 site is more limited by the conformation of the tower loop region than in other MCOs, such as Rigidoporus lignosus laccase (RlL) (45), the BCO T1 site is still capable of accepting electrons from multiple proteinaceous and nonproteinaceous donors (15). The T2/T3 sites are positioned at the subunit-subunit interfaces, similar to the location of the T2 site in NIRs.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of a Two-domain Multicopper Oxidase

Lawton

Sayavedra-Soto

Arp

et al. 2009

Journal of Biological Chemistry

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The two-domain multicopper oxidases are proposed to be key intermediates in the evolution of three-domain multicopper oxidases. A number of two-domain multicopper oxidases have been identified from genome sequences and are classified as type A, type B, or type C on the basis of the predicted location of the type 1 copper center. The crystal structure of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been determined to 1.9 Å resolution. Blue copper oxidase is a trimer, of which each subunit comprises two cupredoxin domains. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The coordination geometry at the trinuclear copper site is consistent with reduction of the copper ions. Although the overall architecture of blue copper oxidase is similar to nitrite reductases, detailed structural alignments show that the fold and domain orientation more closely resemble the three-domain multicopper oxidases. These observations have important implications for the evolution of nitrite reductases and multicopper oxidases. Multicopper oxidases (MCOs)2 are a widely distributed class of enzymes with diverse functions ranging from copper and iron metabolism to polyphenol oxidation. MCOs contain four copper ions arranged in two sites: a blue type 1 mononuclear copper center (T1) and a trinuclear copper cluster (T2/T3) consisting of a normal type 2 copper center (T2) and dinuclear type 3 (T3) center (1-3). Substrate oxidation is coupled to reduction of dioxygen to water via electron transfer from the T1 site to the T2/T3 cluster where dioxygen binds (4, 5). Because of structural similarities, MCOs are often grouped with copper nitrite reductases (NIRs), which contain both T1 and T2 sites (6), and are collectively referred to as multicopper blue proteins (MCBPs) (7). MCOs are composed of multiple cupredoxin domains, and both three-domain and six-domain variants have been studied. Three-domain MCOs (3dMCOs) include ascorbate oxidase, laccases, CueO, and Fet3. In these proteins, the T1 site is located in the C-terminal cupredoxin domain, and the T2/T3 cluster is located at the interface between domains 1 and 3 (8, 9). Ceruloplasmin is a six-domain MCO that houses T1 sites in domains 2, 4, and 6 and a T2/T3 cluster between domains 1 and 6 (10).Because of the prevalence of cupredoxin domains, blue copper proteins, and MCOs in nature, understanding their origins has the potential for addressing important questions about the evolution of protein size, function, structure, and complexity (11). Several models for the evolution of three-and six-domain MCOs have been proposed. In these models, the key evolutionary intermediates are two-domain ancestral MCOs (7,11,12). The two-domain MCOs (2dMCOs) are hypothesized to result from a single domain duplication event and have architectures resembling the homotrimeric two-domain NIRs. NIRs contain a T1 site in each domain 1 and a T2 site at the intersubunit interfaces betwee...

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The Structure of Rigidoporus lignosus Laccase Containing a Full Complement of Copper Ions, Reveals an Asymmetrical Arrangement for the T3 Copper Pair

Cited by 148 publications

References 51 publications

Structural insight into the oxidation of sinapic acid by CotA laccase

Structural insight into the oxidation of sinapic acid by CotA laccase

Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites

Crystal Structure of a Two-domain Multicopper Oxidase

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