Difference between revisions of "Part:BBa K2229450"

Revision as of 07:01, 4 October 2017

Proteorhodopsin (PR) Membrane Receptor

Proteorhodopsin (PR) is a membrane protein of the retinal group commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

Revision as of 10:37, 28 September 2017 (view source) CatY (Talk \| contribs) ← Older edit		Revision as of 07:01, 4 October 2017 (view source) Dylanl18111422 (Talk \| contribs) Newer edit →
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	<partinfo>BBa_K2229450 short</partinfo>		<partinfo>BBa_K2229450 short</partinfo>

−	Proteorhodopsin (PR) is a ~~retinal-binding~~ membrane protein commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.	+	Proteorhodopsin (PR) is a membrane protein of the retinal group commonly known for its function as a light-driven proton pump. This transmembrane protein contains two lysine residue sites - 57 lysine and 59 lysine - that serve as critical citrate-binding sites. The positively charged Lysine residues interact with the negatively charged carboxylate groups, thus inducing a conformational change to the primary structure of PR.