Sandbox Reserved 1598
From Proteopedia
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=== Subunits === | === Subunits === | ||
| - | [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''] bd oxidase is made up of four individual subunits. 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/ | + | [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''] bd oxidase is made up of four individual subunits. 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/4'>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/1'>CydB subunit</scene> harbors the ubiquinone molecule which provides structural support to the subunit that mimics the three hemes found in CydA. 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/2'>CydS subunit</scene> binds to CydA to block oxygen from directly binding to heme b595. The <scene name='83/832924/Cydx_subunit/2'>CydX subunit</scene> promotes the assembly and stability of the oxidase complex. |
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===Q-Loop=== | ===Q-Loop=== | ||
| - | 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. The periplasmic Q-loop in ''E. coli'' | + | 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. 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''. The C-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>. |
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== References == | == References == | ||
| - | <ref name="Ransey">PMID:28504306</ref>. | ||
| - | <ref name="Safarian">PMID: 27126043</ref>. | ||
<references/> | <references/> | ||
Revision as of 01:52, 31 March 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
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References
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
- ↑ 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
- ↑ 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
