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| | <StructureSection load='4u14' size='340' side='right'caption='[[4u14]], [[Resolution|resolution]] 3.57Å' scene=''> | | <StructureSection load='4u14' size='340' side='right'caption='[[4u14]], [[Resolution|resolution]] 3.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u14]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U14 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U14 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u14]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U14 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0HK:(1R,2R,4S,5S,7S)-7-{[HYDROXY(DITHIOPHEN-2-YL)ACETYL]OXY}-9,9-DIMETHYL-3-OXA-9-AZONIATRICYCLO[3.3.1.0~2,4~]NONANE'>0HK</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0HK:(1R,2R,4S,5S,7S)-7-{[HYDROXY(DITHIOPHEN-2-YL)ACETYL]OXY}-9,9-DIMETHYL-3-OXA-9-AZONIATRICYCLO[3.3.1.0~2,4~]NONANE'>0HK</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u15|4u15]], [[4u16|4u16]]</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=4u14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u14 OCA], [https://pdbe.org/4u14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u14 RCSB], [https://www.ebi.ac.uk/pdbsum/4u14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u14 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Chrm3, Chrm-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=4u14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u14 OCA], [http://pdbe.org/4u14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u14 RCSB], [http://www.ebi.ac.uk/pdbsum/4u14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u14 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACM3_RAT ACM3_RAT]] The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.<ref>PMID:1527051</ref> <ref>PMID:1657592</ref> <ref>PMID:22358844</ref> | + | [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> [https://www.uniprot.org/uniprot/ACM3_RAT ACM3_RAT] The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.<ref>PMID:1527051</ref> <ref>PMID:1657592</ref> <ref>PMID:22358844</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4u14" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4u14" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Muscarinic acetylcholine receptor|Muscarinic acetylcholine receptor]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Escherichia virus T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kobilka, B K]] | + | [[Category: Kobilka BK]] |
| - | [[Category: Matt, R A]] | + | [[Category: Matt RA]] |
| - | [[Category: Thorsen, T S]] | + | [[Category: Thorsen TS]] |
| - | [[Category: Weis, W I]] | + | [[Category: Weis WI]] |
| - | [[Category: Alpha helix]]
| + | |
| - | [[Category: Chimera protein]]
| + | |
| - | [[Category: Fusion protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: T4 lysozyme]]
| + | |
| Structural highlights
Function
ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.[1] ACM3_RAT The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.[2] [3] [4]
Publication Abstract from PubMed
G protein-coupled receptors (GPCRs) mediate the majority of cellular responses to hormones and neurotransmitters. Most GPCR crystal structures have been obtained using a fusion protein strategy where the flexible third intracellular loop is replaced by T4 lysozyme (T4L). However, wild-type T4L may not be ideally suited for all GPCRs because of its size and the inherent flexibility between the N- and C-terminal subdomains. Here we report two modified T4L variants, designed to address flexibility and size, that can be used to optimize crystal quality or promote alternative packing interactions. These variants were tested on the M3 muscarinic receptor (M3). The original M3-T4L fusion protein produced twinned crystals that yielded a 3.4 A structure from a 70 crystal data set. We replaced T4L with the modified T4L variants. Both T4L variants yielded M3 muscarinic receptor crystals with alternate lattices that were not twinned, including one that was solved at 2.8 A resolution.
Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-Coupled Receptor Crystallogenesis.,Thorsen TS, Matt R, Weis WI, Kobilka BK Structure. 2014 Oct 23;22(11):1657-1664. doi: 10.1016/j.str.2014.08.022. PMID:25450769[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042
- ↑ Wess J, Maggio R, Palmer JR, Vogel Z. Role of conserved threonine and tyrosine residues in acetylcholine binding and muscarinic receptor activation. A study with m3 muscarinic receptor point mutants. J Biol Chem. 1992 Sep 25;267(27):19313-9. PMID:1527051
- ↑ Wess J, Gdula D, Brann MR. Site-directed mutagenesis of the m3 muscarinic receptor: identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding. EMBO J. 1991 Dec;10(12):3729-34. PMID:1657592
- ↑ Kruse AC, Hu J, Pan AC, Arlow DH, Rosenbaum DM, Rosemond E, Green HF, Liu T, Chae PS, Dror RO, Shaw DE, Weis WI, Wess J, Kobilka BK. Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature. 2012 Feb 22;482(7386):552-6. doi: 10.1038/nature10867. PMID:22358844 doi:10.1038/nature10867
- ↑ Thorsen TS, Matt R, Weis WI, Kobilka BK. Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-Coupled Receptor Crystallogenesis. Structure. 2014 Oct 23;22(11):1657-1664. doi: 10.1016/j.str.2014.08.022. PMID:25450769 doi:http://dx.doi.org/10.1016/j.str.2014.08.022
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