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Thiol dioxygenases all share a common structure described as a 6-stranded β-barrel core, and a canonical cupin or “jelly roll” β-barrel that is formed with cupin motif 1, an intermotif region, and cupin motif 2 each forming two of the core six β-strands in the folded protein structure.<ref>https://www-ncbi-nlm-nih-gov.scd-rproxy.u-strasbg.fr/pmc/articles/PMC3136866/</ref>
Thiol dioxygenases all share a common structure described as a 6-stranded β-barrel core, and a canonical cupin or “jelly roll” β-barrel that is formed with cupin motif 1, an intermotif region, and cupin motif 2 each forming two of the core six β-strands in the folded protein structure.<ref>https://www-ncbi-nlm-nih-gov.scd-rproxy.u-strasbg.fr/pmc/articles/PMC3136866/</ref>
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The Thiol dioxygenase from Pseudomonas aeruginosa is made of 4 chains (named <scene name='75/751223/A/1'>A</scene>, <scene name='75/751223/B/1'>B</scene>, <scene name='75/751223/C/1'>C</scene>, <scene name='75/751223/D/1'>D</scene>)<ref>https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=130072&dps=1</ref>. Each chain is made of 211 amino acids and has a molecular weight of 23 kDa. For its secondary structures, it has <scene name='75/751223/Alpha_helixes/2'>5 alpha helixes</scene> and <scene name='75/751223/Beta_sheets/1'>14 beta sheets</scene>. The different binding sites with an atom of iron<ref>http://www.uniprot.org/uniprot/Q9I0N5</ref> are three different Histidines : <scene name='75/751223/Histidine_89/1'>Histidine 89</scene>, <scene name='75/751223/His_91/1'>Histidine 91</scene> and <scene name='75/751223/His_142/1'>Histidine 142</scene>.
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The Thiol dioxygenase from Pseudomonas aeruginosa is made of 4 chains (named <scene name='75/751223/A/1'>A</scene>, <scene name='75/751223/B/1'>B</scene>, <scene name='75/751223/C/1'>C</scene>, <scene name='75/751223/D/1'>D</scene>)<ref>https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=130072&dps=1</ref>. Each chain is made of 211 amino acids and has a molecular weight of 23 kDa. For its secondary structures, it has <scene name='75/751223/Alpha_helixes/2'>5 alpha helixes</scene> and <scene name='75/751223/Beta_sheets/1'>14 beta sheets</scene><ref>http://www.uniprot.org/uniprot/Q9I0N5</ref>. The different binding sites with an atom of iron are three different Histidines : <scene name='75/751223/Histidine_89/1'>Histidine 89</scene>, <scene name='75/751223/His_91/1'>Histidine 91</scene> and <scene name='75/751223/His_142/1'>Histidine 142</scene>.
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Furthermore, this proteins has two different domains which are a RmlC-like jelly roll fold and a RmlC-like cupin domain.
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Furthermore, this proteins has two different domains which are a RmlC-like jelly roll fold and a RmlC-like cupin domain<ref>http://www.ebi.ac.uk/interpro/protein/Q9I0N5</ref>.

Revision as of 07:47, 26 January 2017

Thiol dioxygenase from Pseudomonas aeruginosa

Structure of one domain of thiol dioxygenase from Pseudomonas aeruginosa (PDB code 4tlf)

Drag the structure with the mouse to rotate

References

  1. https://www-ncbi-nlm-nih-gov.scd-rproxy.u-strasbg.fr/pmc/articles/PMC3136866/
  2. https://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?uid=130072&dps=1
  3. http://www.uniprot.org/uniprot/Q9I0N5
  4. http://www.ebi.ac.uk/interpro/protein/Q9I0N5

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Pierre Rossignol

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