User:Grace A. Bassler/Sandbox 1
From Proteopedia
(Difference between revisions)
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=== Subunits === | === Subunits === | ||
| - | ''E. coli'' bd oxidase is made up of four individual subunits. The two major subunits, CydA and CydB, are both composed of | + | ''E. coli'' bd oxidase is made up of four individual subunits. The two major subunits, CydA and CydB, are both composed of one peripheral helix and two bundles of four transmembrane helices. The <scene name='83/837228/Cyda/3'>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='83/837228/Cydb/1'>CydB subunit</scene> harbors the ubiquinone molecule which provides structural support to the subunit that mimics the three hemes found in CydA. |
| - | <scene name='83/837228/Cyda/3'>CydA Subunit</scene> | ||
| - | |||
| - | <scene name='83/837228/Cydb/1'>CydB Subunit</scene> | ||
<scene name='83/837228/Cyds/1'>CydS Subunit</scene> | <scene name='83/837228/Cyds/1'>CydS Subunit</scene> | ||
Revision as of 00:34, 24 March 2020
bd Oxidase
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References
- ↑ 1.0 1.1 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
- ↑ 2.0 2.1 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
