Cytoglobin: Difference between revisions
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I worked on a project recently researching cytoglobin and I am uploading my findings to proteopedia. |
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==Cytoglobin== | ==Cytoglobin== | ||
<StructureSection load=' | <StructureSection load='2dc3' size='350' side='right' caption='Crystal Structure of Human Cytoglobin at 1.68 Angstroms Resolution' scene=''> | ||
== General Description == | == General Description == | ||
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Cytoglobin is a 44.72 KDa protein, containing 190 amino acids<ref>https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2DC3</ref>. The structure of Cytoglobin is largely alpha helices. The structure also contains a folding pattern characteristic of other globin-like proteins. It contains 8 alpha helices in a 3-over-3 sandwich conformation. CATH classifies each chain of the protein as 1.10.490.103<ref>http://cathdb.info/version/latest/domain/2dc3A00</ref>. | Cytoglobin is a 44.72 KDa protein, containing 190 amino acids<ref>https://www.rcsb.org/pdb/explore/remediatedSequence.do?structureId=2DC3</ref>. The structure of Cytoglobin is largely alpha helices. The structure also contains a folding pattern characteristic of other globin-like proteins. It contains 8 alpha helices in a 3-over-3 sandwich conformation. CATH classifies each chain of the protein as 1.10.490.103<ref>http://cathdb.info/version/latest/domain/2dc3A00</ref>. | ||
The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit disulfide bridge at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | The homodimer is stabilized by electrostatic interactions, hydrogen bonding, and an inter-subunit <scene name='74/748876/Disulfide/1'>disulfide bridge</scene> at CYS38 and CYS832. The most highly conserved residues are the residues involved in the hydrophobic heme pocket, distal and proximal histidine residues, and the inter-subunit disulfide bridge. This is, once again, indicative of potential protein function<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Studies using immunoprecipitation/mass spectrometry did not find any interacting partners of cytoglobin<ref>https://link.springer.com/article/10.1007/s00018-011-0764-9</ref>. Experiments conducted with high concentrations of CYGB have found that it was present only in the monomeric form<ref>https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4925767/</ref>. | ||
== 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 Histidine (His E7) 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/> | ||
