Sandbox Reserved 1598

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===Q-Loop===
===Q-Loop===
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Another significant structural feature of bd oxidase is the <scene name='83/832924/Q_loop/3'>Q-loop</scene> which is located between TM helices 6 and 7 of the CydA subunit.<ref name="Alexander">PMID:31723136</ref> The periplasmic Q-loop in ''E. coli'' stretches over a length of 136 amino acid residues, making it much longer than the Q-loop in ''Geobacillus thermodentrificans''.<ref name="Safarian">PMID: 27126043</ref> The N-terminal end of this Q-loop is very flexible and likely functions as the hinge that allows for quinol binding.<ref name="Alexander">PMID:31723136</ref> The C-terminal end is much more rigid which provides stabilization for the enzyme.
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Another significant structural feature of bd oxidase is the <scene name='83/832924/Q_loop/3'>Q-loop</scene> which is located between TM helices 6 and 7 of the CydA subunit.<ref name="Alexander">PMID:31723136</ref> The periplasmic Q-loop in ''E. coli'' stretches over a length of 136 amino acid residues, making it much longer than the Q-loop in ''Geobacillus thermodentrificans''.<ref name="Safarian">PMID: 27126043</ref> The Q-loop is likely involved in [https://en.wikipedia.org/wiki/Quinone quinone] binding and oxidation. The N-terminal end of this Q-loop is very flexible and likely functions as the hinge that allows for quinone binding while the C-terminal end is much more rigid which provides stabilization for the enzyme.<ref name="Alexander">PMID:31723136</ref>

Revision as of 22:55, 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 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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