Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Voll, Wolfgang; Voit, Renate

doi:10.1073/pnas.87.14.5312

Cited by 24 publications

(8 citation statements)

References 50 publications

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“…The Limulus I1 subunit can be divided into three domains, which, analogous to the Panulirus domain definition, comprise residues 1-154, 155-380, and 381-628, respectively. This agrees reasonably well with the known gene structure of Eurypelma californicum subunit e hemocyanin (Voll & Voit, 1990), where introns were found after residues 65, 141, 210, 342, 385, 430, 492, and 568 (numbers in boldface are close to domain divisions). Schematic diagrams of the Limulus I1 subunit and the three separate domains are given in Figure 5A-D and Kinemages 1-4.…”

Section: Description Of the Structuresupporting

confidence: 89%

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

et al. 1993

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The crystal structure of Limulus polyphemus subunit type I1 hemocyanin in the deoxygenated state has been determined to a resolution of 2.18 A . Phase information for this first structure of a cheliceratan hemocyanin was obtained by molecular replacement using the crustacean hemocyanin structure of Panulirus interruptus. The most striking observation in the Limulus structure is the unexpectedly large distance of 4.6 A between both copper ions in the oxygen-binding site. Each copper has approximate trigonal planar coordination by three histidine NE atoms. No bridging ligand between the copper ions could be detected. Other important new discoveries are (1) the presence of a cis-peptide bond between Glu 309 and Ser 310, with the carbonyl oxygen of the peptide plane hydrogen bonded to the N6 atom of the copper B ligand His 324; (2) localization of a chloride-binding site in the interface between the first and second domain; (3) localization of a putative calcium-binding site in the third domain. Furthermore, comparison of Limulus versus Panulirus hemocyanin revealed considerable tertiary and quaternary rigid body movements, although the overall folds are similar. Within the subunit, the first domain is rotated by about 7.5" with respect to the other two domains, whereas within the hexamer the major movement is a 3.1 O rotation of the trimers with respect to each other. The rigid body rotation of the first domain suggests a structural mechanism for the allosteric regulation by chloride ions and probably causes the cooperative transition of the hexamer between low and high oxygen affinity states. In this postulated mechanism, the fully conserved Phe 49 is the key residue that couples conformational changes of the dinuclear copper site into movements of the first domain.

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Section: Description Of the Structuresupporting

confidence: 89%

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

et al. 1993

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“…Each hemocyanin subunit is folded into three domains with a highly conserved central domain 2 providing the binuclear copper site (CuA, CuB) for binding one oxygen molecule, Nterminal domain 1, and C-terminal domain 3, which are both less stringently conserved among arthropod hemocyanins (9 -11). Moreover, analysis of the exon/intron architecture of one hemocyanin gene supports the proposed protein domain structure (15).…”

mentioning

confidence: 73%

Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum

Voit

Feldmaier-Fuchs²,

Schweikardt

et al. 2000

Journal of Biological Chemistry

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Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. The hemocyanin of the tarantula Eurypelma californicum is a 24-mer protein complex with molecular mass of 1,726,459 Da that consists of seven different polypeptides (a-g), each occupying a distinct position within the native molecule. Here we report the complete molecular structure of the E. californicum hemocyanin as deduced from the corresponding cDNAs. This represents the first complex arthropod hemocyanin to be completely sequenced. The different subunits display 52-66% amino acid sequence identity. Within the subunits, the central domain, which bears the active center with the copper-binding sites A and B, displays the highest degree of identity. Using a homology modeling approach, the putative three-dimensional structure of individual subunits was deduced and compared. Phylogenetic analyses suggest that differentiation of the individual subunits occurred 400 -550 million years ago. The hemocyanin of the stemline Chelicerata was probably a hexamer built up of six distinct subunit types a, b/c, d, e, f, and g, whereas that of the early Arachnida was originally a 24-mer that emerged after the differentiation of subunits b and c.

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“…Those subunits differ considerably in their primary structures and are encoded by distinct genes [34]. In this study, we cloned and characterized the expression pattern of one hemocyanin subunit from M. nipponense (MnHc-1).…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning, Characterization, and mRNA Expression of Hemocyanin Subunit in Oriental River PrawnMacrobrachium nipponense

Kong

Chen

Ding

et al. 2016

International Journal of Genomics

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Hemocyanin is a copper-containing protein with immune function against disease. In this study, a hemocyanin subunit named MnHc-1 was cloned from Macrobrachium nipponense. The full-length cDNA of MnHc-1 was 2,163 bp with a 2,028-bp open reading frame (ORF) encoding a polypeptide of 675 amino acids. The MnHc-1 mRNA was expressed in the hepatopancreas, gill, hemocytes, intestine, ovary, and stomach, with the highest level in the hepatopancreas. In the infection trial, the MnHc-1 mRNA transcripts in the hemocytes were significantly downregulated at 3 h after injection of Aeromonas hydrophila and then upregulated at 6 h and 12 h, followed by a gradual recovery from 24 to 48 h. The MnHc-1 transcriptional expression in the hepatopancreas was measured after M. nipponense were fed seven diets with 2.8, 12.2, 20.9, 29.8, 43.1, 78.9, and 157.1 mg Cu kg−1 for 8 weeks, respectively. The level of MnHc-1 mRNA was significantly higher in the prawns fed 43.1–157.1 mg Cu kg−1 diet than in that fed 2.8–29.8 mg Cu kg−1 diet. This study indicated that the MnHc-1 expression can be affected by dietary copper and the hemocyanin may potentially participate in the antibacterial defense of M. nipponense.

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Characterization of the gene encoding the hemocyanin subunit e from the tarantula Eurypelma californicum.

Cited by 24 publications

References 50 publications

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum

Molecular Cloning, Characterization, and mRNA Expression of Hemocyanin Subunit in Oriental River PrawnMacrobrachium nipponense

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