Hemocyanins

Holde, Kensal E. van; Miller, Karen I.

doi:10.1016/s0065-3233(08)60545-8

Cited by 362 publications

(312 citation statements)

References 193 publications

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“…19 By contrast, the corresponding residues of B. mori SP2 and SP3 are primarily consisted of Tyr residues, which are not capable of copper coordination [ Fig. 6(E-H)].…”

Section: Structural Comparison Of Other Insect Storage Proteinsmentioning

confidence: 99%

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

Hou

et al. 2014

Protein Science

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In holometabolous insects, the accumulation and utilization of storage proteins (SPs), including arylphorins and methionine-rich proteins, are critical for the insect metamorphosis. SPs function as amino acids reserves, which are synthesized in fat body, secreted into the larval hemolymph and taken up by fat body shortly before pupation. However, the detailed molecular mechanisms of digestion and utilization of SPs during development are largely unknown. Here, we report the crystal structure of Bombyx mori arylphorins at 2.8 Å , which displays a heterohexameric structural arrangement formed by trimerization of dimers comprising two structural similar arylphorins. Our limited proteolysis assay and microarray data strongly suggest that papain-like proteases are the major players for B. mori arylphorins digestion in vitro and in vivo. Consistent with the biochemical data, dozens of papain cleavage sites are mapped on the surface of the heterohexameric structure of B. mori arylphorins. Hence, our results provide the insightful information to understand the metamorphosis of holometabolous insects at molecular level.

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“…19 By contrast, the corresponding residues of B. mori SP2 and SP3 are primarily consisted of Tyr residues, which are not capable of copper coordination [ Fig. 6(E-H)].…”

Section: Structural Comparison Of Other Insect Storage Proteinsmentioning

confidence: 99%

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

Hou

et al. 2014

Protein Science

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“…Copper-containing proteins and enzymes play crucial roles in metabolic and cellular processes in both eukaryotes and prokaryotes [1][2][3][4], such as electron transport (plastocyanin, azurin, stellacyanin) [5][6][7], in oxygen transport in arthropods and mollusks (hemocyanin) [8,9], in the reduction of O 2 to H 2 O [cytochrome c oxidase (COX), laccase, ascorbate oxidase] [10], in the reduction of O 2 to H 2 O 2 (amine oxidase, galactose oxidase) [11,12], in the oxidation of various organic substrates (tyrosinase, methane monooxygenase, dopamine b-hydroxylase) [12,13], and in the reduction of small inorganic molecules [nitrite reductase, nitrous oxide reductase (N 2 OR), superoxide dismutase] [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

et al. 2011

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This review focuses on the novel CuZ center of nitrous oxide reductase, an important enzyme owing to the environmental significance of the reaction it catalyzes, reduction of nitrous oxide, and the unusual nature of its catalytic center, named CuZ. The structure of the CuZ center, the unique tetranuclear copper center found in this enzyme, opened a novel area of research in metallobiochemistry. In the last decade, there has been progress in defining the structure of the CuZ center, characterizing the mechanism of nitrous oxide reduction, and identifying intermediates of this reaction. In addition, the determination of the structure of the CuZ center allowed a structural interpretation of the spectroscopic data, which was supported by theoretical calculations. The current knowledge of the structure, function, and spectroscopic characterization of the CuZ center is described here. We would like to stress that although many questions have been answered, the CuZ center remains a scientific challenge, with many hypotheses still being formed.

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“…Between them one molecule oxygen is reversibly bound in side-on (l-g 2 :g 2 ) coordination (4,7,9,10). In most hemocyanins, oxygen binding is highly cooperative and tightly controlled by allosteric effectors (1,2,11,12).…”

Section: Introductionmentioning

confidence: 99%

“…These cylinders either exist as decamers or aggregate further to form didecamers or multidecamers. The mollusc hemocyanin subunit has a molecular mass of 350-400 kDa and is a concatenation of seven or eight paralogous FUs of approximately 50 kDa each (FU-a to FU-h) on a single polypeptide chain (2,16,17). Each FU is typically made-up from two domains and bears one active site.…”

Section: Introductionmentioning

confidence: 99%

The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

et al. 2011

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Hemocyanins are multimeric oxygen‐transport proteins in the hemolymph of many arthropods and mollusks. The overall molecular architecture of arthropod and molluscan hemocyanin is very different, although they possess a similar binuclear type 3 copper center to bind oxygen in a side‐on conformation. Gastropod hemocyanin is a 35 nm cylindrical didecamer (2 × 10‐mer) based on a 400 kDa subunit. The latter is subdivided into eight paralogous “functional units” (FU‐a to FU‐h), each with an active site. FU‐a to FU‐f contribute to the cylinder wall, whereas FU‐g and FU‐h form the internal collar complex. Atomic structures of FU‐e and FU‐g, and a 9 Å cryoEM structure of the 8 MDa didecamer are available. Recently, the structure of keyhole limpet hemocyanin FU‐h (KLH1‐h) was presented as a Cα‐trace at 4 Å resolution. Unlike the other seven FU types, FU‐h contains an additional C‐terminal domain with a cupredoxin‐like fold. Because of the resolution limit of 4 Å, in some loops, the course of the protein backbone could not be established with high certainty yet. Here, we present a refined atomic structure of FU‐h (KLH1‐h) obtained from low‐resolution refinement, which unambiguously establishes the course of the polypeptide backbone and reveals the disulfide bridges as well as the orientation of bulky amino acids. © 2011 IUBMB IUBMB Life, 63(3): 183–187, 2011

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Hemocyanins

Cited by 362 publications

References 193 publications

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

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