User:Grace A. Bassler/Sandbox 1
From Proteopedia
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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 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. | + | ''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. 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='83/837228/Cyds/1'>CydS subunit</scene> binds to CydA to block oxygen from directly binding to heme b595. The <scene name='83/837228/Cydx/1'>CydX subunit</scene> promotes the assembly and stability of the oxidase complex. |
| + | **insert external links!** | ||
| - | <scene name='83/837228/Cyds/1'>CydS Subunit</scene> | ||
| - | |||
| - | <scene name='83/837228/Cydx/1'>CydX Subunit</scene> | ||
===Q Loop=== | ===Q Loop=== | ||
Revision as of 00:42, 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
