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| | <StructureSection load='7bte' size='340' side='right'caption='[[7bte]], [[Resolution|resolution]] 4.20Å' scene=''> | | <StructureSection load='7bte' size='340' side='right'caption='[[7bte]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7bte]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BTE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BTE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bte]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BTE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7bte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bte OCA], [http://pdbe.org/7bte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bte RCSB], [http://www.ebi.ac.uk/pdbsum/7bte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bte ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7bte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bte OCA], [https://pdbe.org/7bte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bte RCSB], [https://www.ebi.ac.uk/pdbsum/7bte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bte ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | + | [https://www.uniprot.org/uniprot/AB140_YEAST AB140_YEAST] S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804, PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1 (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking activity (PubMed:9467951).<ref>PMID:21518804</ref> <ref>PMID:21518805</ref> <ref>PMID:28003514</ref> <ref>PMID:9467951</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides, and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here, we describe the electron cryomicroscopy structures of phalloidin, lifeAct, and utrophin bound to F-actin, providing a comprehensive high-resolution structural comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce specific conformational change and lifeAct specifically recognizes closed D-loop conformation, i.e., ADP-Pi or ADP states of F-actin. The structural models aided designing of minimal utrophin and a shorter lifeAct, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority of actin-binding proteins and thus offering an invaluable resource for researchers in choosing appropriate actin markers and generating new marker variants.
| + | |
| - | | + | |
| - | Structural insights into actin filament recognition by commonly used cellular actin markers.,Kumari A, Kesarwani S, Javoor MG, Vinothkumar KR, Sirajuddin M EMBO J. 2020 Jul 15;39(14):e104006. doi: 10.15252/embj.2019104006. Epub 2020 Jun , 22. PMID:32567727<ref>PMID:32567727</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 7bte" style="background-color:#fffaf0;"></div> | + | |
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| | ==See Also== | | ==See Also== |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kumari, A]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Ragunath, V K]] | + | [[Category: Kumari A]] |
| - | [[Category: Sirajuddin, M]] | + | [[Category: Ragunath VK]] |
| - | [[Category: Adp-f-actin]] | + | [[Category: Sirajuddin M]] |
| - | [[Category: Contractile protein-protein binding complex]]
| + | |
| - | [[Category: F-actin]]
| + | |
| Structural highlights
Function
AB140_YEAST S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804, PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1 (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking activity (PubMed:9467951).[1] [2] [3] [4]
See Also
References
- ↑ D'Silva S, Haider SJ, Phizicky EM. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA. 2011 Jun;17(6):1100-10. PMID:21518804 doi:10.1261/rna.2652611
- ↑ Noma A, Yi S, Katoh T, Takai Y, Suzuki T, Suzuki T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA. 2011 Jun;17(6):1111-9. PMID:21518805 doi:10.1261/rna.2653411
- ↑ Han L, Marcus E, D'Silva S, Phizicky EM. S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. RNA. 2017 Mar;23(3):406-419. PMID:28003514 doi:10.1261/rna.059667.116
- ↑ Asakura T, Sasaki T, Nagano F, Satoh A, Obaishi H, Nishioka H, Imamura H, Hotta K, Tanaka K, Nakanishi H, Takai Y. Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae. Oncogene. 1998 Jan 8;16(1):121-30. PMID:9467951 doi:10.1038/sj.onc.1201487
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