Sandbox Reserved 1607: Difference between revisions
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The selectivity pore is an integral part of the protein. This pore contains a group of glutamate with oxygen facing inward forming a carboxylate ring through which calcium enters. This negative carboxylate ring does a good job of pulling the positive calcium into the selectivity pore at the top of the protein. | The selectivity pore is an integral part of the protein. This pore contains a group of glutamate with oxygen facing inward forming a carboxylate ring through which calcium enters. This negative carboxylate ring does a good job of pulling the positive calcium into the selectivity pore at the top of the protein. | ||
[https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy Cryogenic electron microscopy] (Cryo-EM) was instrumental in outlining the complete structure of this protein. | [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy Cryogenic electron microscopy] (Cryo-EM) was instrumental in outlining the complete structure of this protein. <ref>DOI 10.1038/s41580-018-0052-8</ref> | ||
== Structural highlights and mechanism == | == Structural highlights and mechanism == | ||
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===Selectivity Filter=== | ===Selectivity Filter=== | ||
The <scene name='83/832933/Selectivity_filter/3'>selectivity filter</scene> contains Glu358, Trp354, and Pro359 to allow calcium to pass through the uniporter. The carboxylate oxygen of the <scene name='83/832933/Glu_358/2'>Glu358</scene> side chains draw in the positive calcium ion. The <scene name='83/832933/Diameter/1'>diameter</scene> of the carboxyl ring is about 4Å, allowing only a dehydrated Ca2+ ion to bind. Trp38, which is directly next to the Glu residues, stabilizes the carbonyl side chains through <scene name='83/832933/H_bond_trp354_glu358/2'>hydrogen bonding</scene> and anion pi interactions. These Trp residues also form stacking interactions with Pro359, which orientate the Glu carboxyl side chains towards the middle of the pore to interact with Ca2+ ions. | The <scene name='83/832933/Selectivity_filter/3'>selectivity filter</scene> contains Glu358, Trp354, and Pro359 to allow calcium to pass through the uniporter. The carboxylate oxygen of the <scene name='83/832933/Glu_358/2'>Glu358</scene> side chains draw in the positive calcium ion. The <scene name='83/832933/Diameter/1'>diameter</scene> of the carboxyl ring is about 4Å, allowing only a dehydrated Ca2+ ion to bind. Trp38, which is directly next to the Glu residues, stabilizes the carbonyl side chains through <scene name='83/832933/H_bond_trp354_glu358/2'>hydrogen bonding</scene> and anion pi interactions. These Trp residues also form stacking interactions with Pro359, which orientate the Glu carboxyl side chains towards the middle of the pore to interact with Ca2+ ions. <ref name=”Yoo”>PMID:29954988</ref> | ||
[http://www.rcsb.org/structure/6DT0 Calcium Uniporter Structure] | [http://www.rcsb.org/structure/6DT0 Calcium Uniporter Structure] | ||
== Function == | == Function == | ||
