User:Estelle Blochouse/ Sandbox 1497

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Multicopper oxidase might also be involved in the regulation of metal transport.
Multicopper oxidase might also be involved in the regulation of metal transport.
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Multicopper oxidases are able to oxidise their substrate. They accept an electron in the <scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene> and transfer it to the trinuclear copper centre. The dioxygen binds to the trinuclear center and receive four electrons. It is transformed into two molecules of water.<ref>Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF, Dioxygen reduction by multi-copper oxidases; a structural perspective, November 2005</ref> Three copper centres exist that can be differentiate spectroscopically: Type 1 or blue (<scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene>), type 2 or normal (Cu1004) and type 3 or coupled binuclear (1002 and 1003).<ref>Messerschmidt A, Huber R, The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships, Eur. J. Biochem. 187, January 1990</ref><ref>Ouzounis C, Sander C, A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins, FEBS Lett. volume 279, February 1991</ref>
+
Multicopper oxidases are able to oxidise their substrate. They accept an electron in the <scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene> and transfer it to the trinuclear copper centre. The dioxygen binds to the trinuclear center and receive four electrons. It is transformed into two molecules of water.<ref>Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF, Dioxygen reduction by multi-copper oxidases; a structural perspective, November 2005</ref> Three copper centres exist that can be differentiated spectroscopically: Type 1 or blue (<scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene>), type 2 or normal (Cu1004) and type 3 or coupled binuclear (1002 and 1003).<ref>Messerschmidt A, Huber R, The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships, Eur. J. Biochem. 187, January 1990</ref><ref>Ouzounis C, Sander C, A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins, FEBS Lett. volume 279, February 1991</ref>
== Mechanism ==
== Mechanism ==
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<tr><td>89</td><td>90</td><td>91</td><td>92</td><td>93</td><td>94</td><td>95</td><td>96</td><td>97</td><td>98</td><td>99</td><td>100</td><td>101</td><td>102</td><td class="sblockLbl">103</td><td>104</td><td>105</td><td>106</td><td>107</td><td>108</td><td>109</td><td>110</td><td>111</td><td>112</td><td>113</td><td>114</td><td>115</td><td>116</td><td>117</td><td>118</td></tr>
<tr><td>89</td><td>90</td><td>91</td><td>92</td><td>93</td><td>94</td><td>95</td><td>96</td><td>97</td><td>98</td><td>99</td><td>100</td><td>101</td><td>102</td><td class="sblockLbl">103</td><td>104</td><td>105</td><td>106</td><td>107</td><td>108</td><td>109</td><td>110</td><td>111</td><td>112</td><td>113</td><td>114</td><td>115</td><td>116</td><td>117</td><td>118</td></tr>
<tr><td>D</td><td>I</td><td>Y</td><td>N</td><td>Q</td><td>L</td><td>T</td><td>E</td><td>E</td><td>T</td><td>T</td><td>L</td><td>H</td><td>W</td><td class="sblockLbl">H</td><td>G</td><td>L</td><td>E</td><td>V</td><td>P</td><td>G</td><td>E</td><td>V</td><td>D</td><td>G</td><td>G</td><td>P</td><td>Q</td><td>G</td><td>I</td></tr>
<tr><td>D</td><td>I</td><td>Y</td><td>N</td><td>Q</td><td>L</td><td>T</td><td>E</td><td>E</td><td>T</td><td>T</td><td>L</td><td>H</td><td>W</td><td class="sblockLbl">H</td><td>G</td><td>L</td><td>E</td><td>V</td><td>P</td><td>G</td><td>E</td><td>V</td><td>D</td><td>G</td><td>G</td><td>P</td><td>Q</td><td>G</td><td>I</td></tr>
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<tr><td>119</td><td>120</td><td>121</td><td>122</td><td>123</td><td>124</td><td>125</td><td>126</td><td>127</td><td>128</td><td>129</td><td>130</td><td>131</td><td>132</td><td>133</td><td>134</td><td>135</td><td>136</td><td>137</td><td>138</td><td>139</td><td>140</td><td class="sblockLbl">141</td><td>142</td><td class="FFC0CB">143</td><td>144</td><td>145</td><td>146</td><td>147</td><td>148</td></tr>
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<tr><td>119</td><td>120</td><td>121</td><td>122</td><td>123</td><td>124</td><td>125</td><td>126</td><td>127</td><td>128</td><td>129</td><td>130</td><td>131</td><td>132</td><td>133</td><td>134</td><td>135</td><td>136</td><td>137</td><td>138</td><td>139</td><td>140</td><td class="sblockLbl">141</td><td>142</td><td color="FFC0CB">143</td><td>144</td><td>145</td><td>146</td><td>147</td><td>148</td></tr>
<tr><td>I</td><td>P</td><td>P</td><td>G</td><td>G</td><td>K</td><td>R</td><td>S</td><td>V</td><td>T</td><td>L</td><td>N</td><td>V</td><td>D</td><td>Q</td><td>P</td><td>A</td><td>A</td><td>T</td><td>C</td><td>W</td><td>F</td><td class="sblockLbl">H</td><td>P</td><td color="FFC0CB">H</td><td>Q</td><td>H</td><td>G</td><td>K</td><td>T</td></tr>
<tr><td>I</td><td>P</td><td>P</td><td>G</td><td>G</td><td>K</td><td>R</td><td>S</td><td>V</td><td>T</td><td>L</td><td>N</td><td>V</td><td>D</td><td>Q</td><td>P</td><td>A</td><td>A</td><td>T</td><td>C</td><td>W</td><td>F</td><td class="sblockLbl">H</td><td>P</td><td color="FFC0CB">H</td><td>Q</td><td>H</td><td>G</td><td>K</td><td>T</td></tr>
<tr><td>149</td><td>150</td><td>151</td><td>152</td><td>153</td><td>154</td><td>155</td><td>156</td><td>157</td><td>158</td><td>159</td><td>160</td><td>161</td><td>162</td><td>163</td><td>164</td><td>165</td><td>166</td><td>167</td><td>168</td><td>169</td><td>170</td><td>171</td><td>172</td><td>173</td><td>174</td><td>175</td><td>176</td><td>177</td><td>178</td></tr>
<tr><td>149</td><td>150</td><td>151</td><td>152</td><td>153</td><td>154</td><td>155</td><td>156</td><td>157</td><td>158</td><td>159</td><td>160</td><td>161</td><td>162</td><td>163</td><td>164</td><td>165</td><td>166</td><td>167</td><td>168</td><td>169</td><td>170</td><td>171</td><td>172</td><td>173</td><td>174</td><td>175</td><td>176</td><td>177</td><td>178</td></tr>

Revision as of 16:15, 11 January 2019

Multicopper Oxidase CueO (4e9s)

4e9s, resolution 1.06Å

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References

  1. ↑ EMBL-EBI, Family: Cu-oxidase (PF00394), Summary: Multicopper oxidase, http://pfam.xfam.org/family/Cu-oxidase
  2. ↑ UniProtKB
  3. ↑ Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF, Dioxygen reduction by multi-copper oxidases; a structural perspective, November 2005
  4. ↑ Messerschmidt A, Huber R, The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships, Eur. J. Biochem. 187, January 1990
  5. ↑ Ouzounis C, Sander C, A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins, FEBS Lett. volume 279, February 1991
  6. ↑ Hirofumi Komori, Ryosuke Sugiyama, Kunishige Kataoka, Kentaro Miyazaki, Yoshiki Higuchib, and Takeshi Sakurai, New insights into the catalytic active-site structure of multicopper oxidases, Biological Crystallography, 6 December 2013 doi:10.1107/S1399004713033051
  7. ↑ RCBS PDB
  8. ↑ RCBS PDB
  9. ↑ RCBS PDB
  10. ↑ RCBS PDB
  11. ↑ RCBS PDB
  12. ↑ RCBS PDB
  13. ↑ Kataoka K, Komori H, Ueki Y, Konno Y, Kamitaka Y, Kurose S, Tsujimura S, Higuchi Y, Kano K, Seo D, Sakurai T. Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site. J Mol Biol. 2007 Oct 12;373(1):141-52. Epub 2007 Aug 2. PMID:17804014 doi:10.1016/j.jmb.2007.07.041

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Estelle Blochouse

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