Sandbox Reserved 1616: Difference between revisions
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[[Image: 5doq_WHOLE_IMAGE.png|300 px|left|thumb|Figure 2: 6RX4 monomer subunit; alpha helices in teal, beta sheets in purple.]] | [[Image: 5doq_WHOLE_IMAGE.png|300 px|left|thumb|Figure 2: 6RX4 monomer subunit; alpha helices in teal, beta sheets in purple.]] | ||
{{Clear}} | {{Clear}} | ||
This page will be specifically focusing on the structure and overall function of the 6RX4 bd oxidase. 6RX4 is a part of the long(L) quinol-binding domain subfamily that terminal oxidases are classified into. The L-subfamily of bd oxidases are responsible for the survival of acute infectious diseases such as E.Coli and salmonella. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed Q loop, and four protein subunits will be of primary focus when identifying the relationship between structure and function. | This page will be specifically focusing on the structure and overall function of the 6RX4 bd oxidase. 6RX4 is a part of the long(L) quinol-binding domain subfamily that terminal oxidases are classified into. The L-subfamily of bd oxidases are responsible for the survival of acute infectious diseases such as E.Coli and salmonella. The 6RX4's three <scene name='83/832931/Heme/4'>heme</scene> groups, its periplasmically exposed <scene name='83/832924/Q_loop/3'>Q-loop</scene>, and four protein subunits will be of primary focus when identifying the relationship between structure and function. | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
[[Image:Q Loop.png|400 px|right|thumb|Figure 1]] | [[Image:Q Loop.png|400 px|right|thumb|Figure 1]] | ||
