This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4a4m

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:44, 18 August 2022

Crystal structure of the light-activated constitutively active N2C, M257Y,D282C rhodopsin mutant in complex with a peptide resembling the C-terminus of the Galpha-protein subunit (GaCT)

Structural highlights

4a4m is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Related:	1ov0, 1n3m, 2i37, 1bok, 2i36, 1edx, 2j4y, 1vqx, 1ln6, 1jfp, 1ov1, 1f88, 1boj, 1nzs, 1eds, 2x72, 1u19, 1fdf, 1edw, 1hzx, 2i35, 1l9h, 1gzm, 1edv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OPSD_BOVIN] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).^[1] ^[2] [GNAT3_BOVIN] Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction.

Publication Abstract from PubMed

G protein-coupled receptors (GPCR) are seven transmembrane helix proteins that couple binding of extracellular ligands to conformational changes and activation of intracellular G proteins, GPCR kinases, and arrestins. Constitutively active mutants are ubiquitously found among GPCRs and increase the inherent basal activity of the receptor, which often correlates with a pathological outcome. Here, we have used the M257Y(6.40) constitutively active mutant of the photoreceptor rhodopsin in combination with the specific binding of a C-terminal fragment from the G protein alpha subunit (GalphaCT) to trap a light activated state for crystallization. The structure of the M257Y/GalphaCT complex contains the agonist all-trans-retinal covalently bound to the native binding pocket and resembles the G protein binding metarhodopsin-II conformation obtained by the natural activation mechanism; i.e., illumination of the prebound chromophore 11-cis-retinal. The structure further suggests a molecular basis for the constitutive activity of 6.40 substitutions and the strong effect of the introduced tyrosine based on specific interactions with Y223(5.58) in helix 5, Y306(7.53) of the NPxxY motif and R135(3.50) of the E(D)RY motif, highly conserved residues of the G protein binding site.

Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II.,Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, Standfuss J Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):119-24. Epub 2011 Dec 23. PMID:22198838^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakamichi H, Okada T. Local peptide movement in the photoreaction intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Aug 22;103(34):12729-34. Epub 2006 Aug 14. PMID:16908857
↑ Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, Palczewski K. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16123-8. Epub 2006 Oct 23. PMID:17060607
↑ Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, Standfuss J. Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):119-24. Epub 2011 Dec 23. PMID:22198838 doi:10.1073/pnas.1114089108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a4m"

@@ Line 3: / Line 3: @@
 <StructureSection load='4a4m' size='340' side='right'caption='[[4a4m]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a4m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A4M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a4m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ov0|1ov0]], [[1n3m|1n3m]], [[2i37|2i37]], [[1bok|1bok]], [[2i36|2i36]], [[1edx|1edx]], [[2j4y|2j4y]], [[1vqx|1vqx]], [[1ln6|1ln6]], [[1jfp|1jfp]], [[1ov1|1ov1]], [[1f88|1f88]], [[1boj|1boj]], [[1nzs|1nzs]], [[1eds|1eds]], [[2x72|2x72]], [[1u19|1u19]], [[1fdf|1fdf]], [[1edw|1edw]], [[1hzx|1hzx]], [[2i35|2i35]], [[1l9h|1l9h]], [[1gzm|1gzm]], [[1edv|1edv]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ov0|1ov0]], [[1n3m|1n3m]], [[2i37|2i37]], [[1bok|1bok]], [[2i36|2i36]], [[1edx|1edx]], [[2j4y|2j4y]], [[1vqx|1vqx]], [[1ln6|1ln6]], [[1jfp|1jfp]], [[1ov1|1ov1]], [[1f88|1f88]], [[1boj|1boj]], [[1nzs|1nzs]], [[1eds|1eds]], [[2x72|2x72]], [[1u19|1u19]], [[1fdf|1fdf]], [[1edw|1edw]], [[1hzx|1hzx]], [[2i35|2i35]], [[1l9h|1l9h]], [[1gzm|1gzm]], [[1edv|1edv]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4m OCA], [http://pdbe.org/4a4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a4m RCSB], [http://www.ebi.ac.uk/pdbsum/4a4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4m ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4m OCA], [https://pdbe.org/4a4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4m RCSB], [https://www.ebi.ac.uk/pdbsum/4a4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4m ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN]] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref>  [[http://www.uniprot.org/uniprot/GNAT3_BOVIN GNAT3_BOVIN]] Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction.
+[[https://www.uniprot.org/uniprot/OPSD_BOVIN OPSD_BOVIN]] Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change leading to G-protein activation and release of all-trans retinal (By similarity).<ref>PMID:16908857</ref> <ref>PMID:17060607</ref>  [[https://www.uniprot.org/uniprot/GNAT3_BOVIN GNAT3_BOVIN]] Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 ==See Also==
-*[[Rhodopsin|Rhodopsin]]
+*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
 == References ==
 <references/>

4a4m

From Proteopedia

Revision as of 07:44, 18 August 2022

Crystal structure of the light-activated constitutively active N2C, M257Y,D282C rhodopsin mutant in complex with a peptide resembling the C-terminus of the Galpha-protein subunit (GaCT)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox