Sandbox Reserved 1598

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=== Subunits ===
=== Subunits ===
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[https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''] bd oxidase is made up of four individual subunits.<ref name="Alexander">PMID:31723136</ref> The two major subunits, CydA and CydB, are each composed of one peripheral helix and two bundles of four transmembrane helices. The <scene name='83/832924/Cyda_subunit/5'>CydA subunit</scene> plays the most important role in the oxygen reduction reaction as it contains the Q-loop as well as all three heme groups. The <scene name='83/832924/Cydb_subunit/2'>CydB subunit</scene> harbors the <scene name='83/832924/Ubiquinone/3'>ubiquinone</scene> molecule which provides structural support to the subunit that mimics the three hemes found in CydA.<ref name="Safarian">PMID: 31604309</ref><ref name="Safarian2">PMID: 27126043</ref> The remaining two subunits, CydS and CydX, are both single helix structures that assist in the oxygen reduction reaction. Unique to ''E. coli'', the <scene name='83/832924/Cyds_subunit/3'>CydS subunit</scene> binds to CydA to block oxygen from directly binding to heme b595. The <scene name='83/832924/Cydx_subunit/3'>CydX subunit</scene> promotes the assembly and stability of the oxidase complex. CydX is composed of 37 mostly hydrophilic amino acid residues, including <scene name='83/832924/Glu25/1'>Glu25</scene> that is exposed to the cytoplasm and prevents the helix from fully entering the membrane.
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[https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''] bd oxidase is made up of four individual subunits.<ref name="Alexander">PMID:31723136</ref> The two major subunits, CydA and CydB, are each composed of one peripheral helix and two bundles of four transmembrane helices. The <scene name='83/832924/Cyda_subunit/5'>CydA subunit</scene> plays the most important role in the oxygen reduction reaction as it contains the Q-loop as well as all three heme groups. The <scene name='83/832924/Cydb_subunit/2'>CydB subunit</scene> harbors the <scene name='83/832924/Ubiquinone/3'>ubiquinone</scene> molecule which provides structural support to the subunit that mimics the three hemes found in CydA.<ref name="Safarian">PMID: 31604309</ref><ref name="Safarian2">PMID: 27126043</ref> The remaining two subunits, CydS and CydX, are both single helix structures that assist in the oxygen reduction reaction. Unique to ''E. coli'', the <scene name='83/832924/Cyds_subunit/3'>CydS subunit</scene> binds to CydA to block oxygen from directly binding to heme b595. The <scene name='83/832924/Cydx_subunit/3'>CydX subunit</scene> promotes the assembly and stability of the oxidase complex. CydX is composed of 37 mostly hydrophilic amino acid residues, including <scene name='83/832924/Glu25/2'>Glu25</scene> that is exposed to the cytoplasm and prevents the helix from fully entering the membrane. <ref name="Alexander">PMID:31723136</ref>

Revision as of 23:23, 6 April 2020

User: Grace A. Bassler/Sandbox 1

This Sandbox is Reserved from Jan 13 through September 1, 2020 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1598 through Sandbox Reserved 1627.
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bd Oxidase

bd Oxidase: 6RX4. Cryo-EM structure of bd oxidase from E. coli.

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References

  1. ↑ 1.0 1.1 1.2 1.3 Thesseling A, Rasmussen T, Burschel S, Wohlwend D, Kagi J, Muller R, Bottcher B, Friedrich T. Homologous bd oxidases share the same architecture but differ in mechanism. Nat Commun. 2019 Nov 13;10(1):5138. doi: 10.1038/s41467-019-13122-4. PMID:31723136 doi:http://dx.doi.org/10.1038/s41467-019-13122-4
  2. ↑ 2.0 2.1 Safarian S, Hahn A, Mills DJ, Radloff M, Eisinger ML, Nikolaev A, Meier-Credo J, Melin F, Miyoshi H, Gennis RB, Sakamoto J, Langer JD, Hellwig P, Kuhlbrandt W, Michel H. Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science. 2019 Oct 4;366(6461):100-104. doi: 10.1126/science.aay0967. PMID:31604309 doi:http://dx.doi.org/10.1126/science.aay0967
  3. ↑ Safarian S, Rajendran C, Muller H, Preu J, Langer JD, Ovchinnikov S, Hirose T, Kusumoto T, Sakamoto J, Michel H. Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases. Science. 2016 Apr 29;352(6285):583-6. doi: 10.1126/science.aaf2477. PMID:27126043 doi:http://dx.doi.org/10.1126/science.aaf2477
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