Cytoglobin: Difference between revisions
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== Structural Insights into Function == | == Structural Insights into Function == | ||
Cytoglobin’s structure, particularly the heme group, contributes to its function greatly. In the deoxygenated form of cytoglobin, the heme group is coordinated with endogenous ligands at all 6 sites of the heme group, with the 6th site being occupied by a distal<scene name='74/748876/His_residues/1'> Histidine (His E7)</scene> residue on the protein. Oxygen competes with this His residue to bind CYGB<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | Cytoglobin’s structure, particularly the heme group, contributes to its function greatly. In the deoxygenated form of cytoglobin, the heme group is coordinated with endogenous ligands at all 6 sites of the<scene name='74/748876/Hemegroup/2'> heme</scene> group, with the 6th site being occupied by a distal<scene name='74/748876/His_residues/1'> Histidine (His E7)</scene> residue on the protein. Oxygen competes with this His residue to bind CYGB<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | ||
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==Evolutionarily Related Proteins== | ==Evolutionarily Related Proteins== | ||
[[Myoglobin]] has very high homology, and it is suggested that | [[Myoglobin]] has very high homology, and it is suggested that CYGB emerged from a large scale duplication event<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>.[[ Hemoglobin]] also has high homology, with a query cover of 77% following a BLAST search using the Uniprot/SwissKB database<ref>https://blast.ncbi.nlm.nih.gov/Blast.cgi</ref>. | ||
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[[1urv]], [[1ury]], [[1ut0]], [[1ux9]] – hCYGB (mutant) + Fe(CN)6 <br /> | [[1urv]], [[1ury]], [[1ut0]], [[1ux9]] – hCYGB (mutant) + Fe(CN)6 <br /> | ||
[[4b3w]] – hCYGB (mutant) + CN + Fe(CN)6 <br /> | [[4b3w]] – hCYGB (mutant) + CN + Fe(CN)6 <br /> | ||
[[6q6p]] – CYGB (mutant) – Antarctic toothfish<br /> | |||
== References == | == References == | ||
<references/> | <references/> | ||