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Structure of the processive rubber oxygenase RoxA from Xanthomonas sp
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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| Personen und Körperschaften: | , , , , |
| In: | Proceedings of the National Academy of Sciences, 110, 2013, 34, S. 13833-13838 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver |
|---|---|
| author |
Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver |
| spellingShingle |
Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver Proceedings of the National Academy of Sciences Structure of the processive rubber oxygenase RoxA from Xanthomonas sp Multidisciplinary |
| author_sort |
seidel, julian |
| spelling |
Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1305560110 <jats:p> Rubber oxygenase A (RoxA) is one of only two known enzymes able to catalyze the oxidative cleavage of latex for biodegradation. RoxA acts as a processive dioxygenase to yield the predominant product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD), a tri-isoprene unit. Here we present a structural analysis of RoxA from <jats:italic>Xanthomonas</jats:italic> sp. strain 35Y at a resolution of 1.8 Å. The enzyme is a 75-kDa diheme <jats:italic>c</jats:italic> -type cytochrome with an unusually low degree of secondary structure. Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinship with diheme peroxidases of the CcpA family, but the proteins are functionally distinct, and the extracellular RoxA has evolved to have twice the molecular mass by successively accumulating extensions of peripheral loops. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we show that RoxA is isolated with O <jats:sub>2</jats:sub> stably bound to the active site heme iron. Activation and cleavage of O <jats:sub>2</jats:sub> require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage. </jats:p> Structure of the processive rubber oxygenase RoxA from <i>Xanthomonas</i> sp Proceedings of the National Academy of Sciences |
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| title |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_unstemmed |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_full |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_fullStr |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_full_unstemmed |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_short |
Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_sort |
structure of the processive rubber oxygenase roxa from
<i>xanthomonas</i>
sp |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1305560110 |
| publishDate |
2013 |
| physical |
13833-13838 |
| description |
<jats:p>
Rubber oxygenase A (RoxA) is one of only two known enzymes able to catalyze the oxidative cleavage of latex for biodegradation. RoxA acts as a processive dioxygenase to yield the predominant product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD), a tri-isoprene unit. Here we present a structural analysis of RoxA from
<jats:italic>Xanthomonas</jats:italic>
sp. strain 35Y at a resolution of 1.8 Å. The enzyme is a 75-kDa diheme
<jats:italic>c</jats:italic>
-type cytochrome with an unusually low degree of secondary structure. Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinship with diheme peroxidases of the CcpA family, but the proteins are functionally distinct, and the extracellular RoxA has evolved to have twice the molecular mass by successively accumulating extensions of peripheral loops. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we show that RoxA is isolated with O
<jats:sub>2</jats:sub>
stably bound to the active site heme iron. Activation and cleavage of O
<jats:sub>2</jats:sub>
require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage.
</jats:p> |
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| author | Seidel, Julian, Schmitt, Georg, Hoffmann, Maren, Jendrossek, Dieter, Einsle, Oliver |
| author_facet | Seidel, Julian, Schmitt, Georg, Hoffmann, Maren, Jendrossek, Dieter, Einsle, Oliver, Seidel, Julian, Schmitt, Georg, Hoffmann, Maren, Jendrossek, Dieter, Einsle, Oliver |
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| description | <jats:p> Rubber oxygenase A (RoxA) is one of only two known enzymes able to catalyze the oxidative cleavage of latex for biodegradation. RoxA acts as a processive dioxygenase to yield the predominant product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD), a tri-isoprene unit. Here we present a structural analysis of RoxA from <jats:italic>Xanthomonas</jats:italic> sp. strain 35Y at a resolution of 1.8 Å. The enzyme is a 75-kDa diheme <jats:italic>c</jats:italic> -type cytochrome with an unusually low degree of secondary structure. Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinship with diheme peroxidases of the CcpA family, but the proteins are functionally distinct, and the extracellular RoxA has evolved to have twice the molecular mass by successively accumulating extensions of peripheral loops. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we show that RoxA is isolated with O <jats:sub>2</jats:sub> stably bound to the active site heme iron. Activation and cleavage of O <jats:sub>2</jats:sub> require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage. </jats:p> |
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| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| physical | 13833-13838 |
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| spelling | Seidel, Julian Schmitt, Georg Hoffmann, Maren Jendrossek, Dieter Einsle, Oliver 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1305560110 <jats:p> Rubber oxygenase A (RoxA) is one of only two known enzymes able to catalyze the oxidative cleavage of latex for biodegradation. RoxA acts as a processive dioxygenase to yield the predominant product 12-oxo-4,8-dimethyl-trideca-4,8-diene-1-al (ODTD), a tri-isoprene unit. Here we present a structural analysis of RoxA from <jats:italic>Xanthomonas</jats:italic> sp. strain 35Y at a resolution of 1.8 Å. The enzyme is a 75-kDa diheme <jats:italic>c</jats:italic> -type cytochrome with an unusually low degree of secondary structure. Analysis of the heme group arrangement and peptide chain topology of RoxA confirmed a distant kinship with diheme peroxidases of the CcpA family, but the proteins are functionally distinct, and the extracellular RoxA has evolved to have twice the molecular mass by successively accumulating extensions of peripheral loops. RoxA incorporates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we show that RoxA is isolated with O <jats:sub>2</jats:sub> stably bound to the active site heme iron. Activation and cleavage of O <jats:sub>2</jats:sub> require binding of polyisoprene, and thus the substrate needs to use hydrophobic access channels to reach the deeply buried active site of RoxA. The location and nature of these channels support a processive mechanism of latex cleavage. </jats:p> Structure of the processive rubber oxygenase RoxA from <i>Xanthomonas</i> sp Proceedings of the National Academy of Sciences |
| spellingShingle | Seidel, Julian, Schmitt, Georg, Hoffmann, Maren, Jendrossek, Dieter, Einsle, Oliver, Proceedings of the National Academy of Sciences, Structure of the processive rubber oxygenase RoxA from Xanthomonas sp, Multidisciplinary |
| title | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_full | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_fullStr | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_full_unstemmed | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_short | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| title_sort | structure of the processive rubber oxygenase roxa from <i>xanthomonas</i> sp |
| title_unstemmed | Structure of the processive rubber oxygenase RoxA from Xanthomonas sp |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1305560110 |