User:Eduardo Araujo Silva/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
== Structural highlights ==
== Structural highlights ==
-
In the absence of an ORx, Orco is capable of forming a <scene name='10/1050291/Homotetramer/1'>homotetramer</scene>, with four subunits encircling a channel. Each <scene name='10/1050291/Subunit/1'>subunit</scene> is composed of 7 transmembrane domains (S1-S7), an intracellular <FONT COLOR="blue">'''N-terminus'''</FONT> and an extracellular <FONT COLOR="red">'''C-terminus'''</FONT>. <scene name='10/1050291/S7/1'>S7</scene> is divided into a cytoplasmic helix (S7a) and a transmembrane helix (S7b), separated by a 15-residue β-hairpin loop. The majority of the protein is intramembranous, while <scene name='10/1050291/Small_loops/2'>small loops</scene> are exposed to the extracellular environment, and a small intracellular domain, called the anchor domain, extends into the cytoplasm. The anchor domain is named as such because its where the majority of <scene name='10/1050291/Inter-subunit_interaction/2'>inter-subunit interactions</scene> resides and thus 'anchoring' the subunits within the lipid membrane. In the core of the anchor domain is S7a surrounded by S4, S5 and S6. The S1-S6 domains of each subunit are narrowly tethered to their respective S7b helix and are separated from the domains of the other subunits. Each subunit contributes with a <scene name='10/1050291/S7b/2'>S7b helix</scene> that lines the ion-conduction pathway. The pore is narrowest near the extracellular end, where two residues, Leu 473 and Val 469, forms a <scene name='10/1050291/Constriction/2'>constriction</scene>, preventing the passage of hydrated ions, which characterizes its closed state <ref>PMID: 30111839</ref>.
+
In the absence of an ORx, Orco is capable of forming a <scene name='10/1050291/Homotetramer/1'>homotetramer</scene>, with four subunits encircling a channel. Each <scene name='10/1050291/Subunit/1'>subunit</scene> is composed of 7 transmembrane domains (S1-S7), an intracellular <FONT COLOR="blue">'''N-terminus'''</FONT> and an extracellular <FONT COLOR="red">'''C-terminus'''</FONT>. <scene name='10/1050291/S7/2'>S7</scene> is divided into a cytoplasmic helix (S7a) and a transmembrane helix (S7b), separated by a 15-residue β-hairpin loop. The majority of the protein is intramembranous, while <scene name='10/1050291/Small_loops/2'>small loops</scene> are exposed to the extracellular environment, and a small intracellular domain, called the anchor domain, extends into the cytoplasm. The anchor domain is named as such because its where the majority of <scene name='10/1050291/Inter-subunit_interaction/2'>inter-subunit interactions</scene> resides and thus 'anchoring' the subunits within the lipid membrane. In the core of the anchor domain is S7a surrounded by S4, S5 and S6. The S1-S6 domains of each subunit are narrowly tethered to their respective S7b helix and are separated from the domains of the other subunits. Each subunit contributes with a <scene name='10/1050291/S7b/2'>S7b helix</scene> that lines the ion-conduction pathway. The pore is narrowest near the extracellular end, where two residues, Leu 473 and Val 469, forms a <scene name='10/1050291/Constriction/2'>constriction</scene>, preventing the passage of hydrated ions, which characterizes its closed state <ref>PMID: 30111839</ref>.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 02:39, 2 June 2024

Orco (6c70)

Cryo-EM structure of Orco homotetramer from the parasitic fig wasp Apocrypta bakeri at 3.5 Å resolution 6c70

Drag the structure with the mouse to rotate

References

  1. Larsson MC, Domingos AI, Jones WD, Chiappe ME, Amrein H, Vosshall LB. Or83b encodes a broadly expressed odorant receptor essential for Drosophila olfaction. Neuron. 2004 Sep 2;43(5):703-14. PMID:15339651 doi:http://dx.doi.org/10.1016/j.neuron.2004.08.019
  2. Jones WD, Nguyen TA, Kloss B, Lee KJ, Vosshall LB. Functional conservation of an insect odorant receptor gene across 250 million years of evolution. Curr Biol. 2005 Feb 22;15(4):R119-21. PMID:15723778 doi:10.1016/j.cub.2005.02.007
  3. Benton R, Sachse S, Michnick SW, Vosshall LB. Atypical membrane topology and heteromeric function of Drosophila odorant receptors in vivo. PLoS Biol. 2006 Feb;4(2):e20. PMID:16402857 doi:10.1371/journal.pbio.0040020
  4. Larsson MC, Domingos AI, Jones WD, Chiappe ME, Amrein H, Vosshall LB. Or83b encodes a broadly expressed odorant receptor essential for Drosophila olfaction. Neuron. 2004 Sep 2;43(5):703-14. PMID:15339651 doi:http://dx.doi.org/10.1016/j.neuron.2004.08.019
  5. Jones PL, Pask GM, Rinker DC, Zwiebel LJ. Functional agonism of insect odorant receptor ion channels. Proc Natl Acad Sci U S A. 2011 May 24;108(21):8821-5. PMID:21555561 doi:10.1073/pnas.1102425108
  6. Butterwick JA, Del Marmol J, Kim KH, Kahlson MA, Rogow JA, Walz T, Ruta V. Cryo-EM structure of the insect olfactory receptor Orco. Nature. 2018 Aug;560(7719):447-452. doi: 10.1038/s41586-018-0420-8. Epub 2018 Aug, 15. PMID:30111839 doi:http://dx.doi.org/10.1038/s41586-018-0420-8

Proteopedia Page Contributors and Editors (what is this?)

Eduardo Araujo Silva

Personal tools