7dhw

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<StructureSection load='7dhw' size='340' side='right'caption='[[7dhw]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
<StructureSection load='7dhw' size='340' side='right'caption='[[7dhw]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7dhw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DHW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7dhw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DHW FirstGlance]. <br>
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</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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XI-2, MYA2, At5g43900, F6B6.4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7dhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dhw OCA], [https://pdbe.org/7dhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dhw RCSB], [https://www.ebi.ac.uk/pdbsum/7dhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dhw 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=7dhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dhw OCA], [https://pdbe.org/7dhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dhw RCSB], [https://www.ebi.ac.uk/pdbsum/7dhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dhw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MYO6_ARATH MYO6_ARATH]] Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in the tip growth of root hair cells. Plays a major role in trafficking of Golgi stacks, mitochondria and peroxisomes during root hair development. Targets the peroxisome through an interaction with RABC2A. Required for development of pavement cells, trichomes, and stigmatic papillae.<ref>PMID:15792961</ref> <ref>PMID:18178669</ref> <ref>PMID:19060218</ref> <ref>PMID:19369591</ref> <ref>PMID:20581304</ref> <ref>PMID:21914656</ref> <ref>PMID:22672737</ref>
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[https://www.uniprot.org/uniprot/MYO6_ARATH MYO6_ARATH] Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Involved in the tip growth of root hair cells. Plays a major role in trafficking of Golgi stacks, mitochondria and peroxisomes during root hair development. Targets the peroxisome through an interaction with RABC2A. Required for development of pavement cells, trichomes, and stigmatic papillae.<ref>PMID:15792961</ref> <ref>PMID:18178669</ref> <ref>PMID:19060218</ref> <ref>PMID:19369591</ref> <ref>PMID:20581304</ref> <ref>PMID:21914656</ref> <ref>PMID:22672737</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytoplasmic streaming with extremely high velocity ( approximately 70 mum s(-1)) occurs in cells of the characean algae (Chara). Because cytoplasmic streaming is caused by myosin XI, it has been suggested that a myosin XI with a velocity of 70 mum s(-1), the fastest myosin measured so far, exists in Chara cells. However, the velocity of the previously cloned Chara corallina myosin XI (CcXI) was about 20 mum s(-1), one-third of the cytoplasmic streaming velocity in Chara Recently, the genome sequence of Chara braunii has been published, revealing that this alga has four myosin XI genes. We cloned these four myosin XI (CbXI-1, 2, 3, and 4) and measured their velocities. While the velocities of CbXI-3 and CbXI-4 motor domains (MDs) were similar to that of CcXI MD, the velocities of CbXI-1 and CbXI-2 MDs were 3.2 times and 2.8 times faster than that of CcXI MD, respectively. The velocity of chimeric CbXI-1, a functional, full-length CbXI-1 construct, was 60 mum s(-1) These results suggest that CbXI-1 and CbXI-2 would be the main contributors to cytoplasmic streaming in Chara cells and show that these myosins are ultrafast myosins with a velocity 10 times faster than fast skeletal muscle myosins in animals. We also report an atomic structure (2.8-A resolution) of myosin XI using X-ray crystallography. Based on this crystal structure and the recently published cryo-electron microscopy structure of acto-myosin XI at low resolution (4.3-A), it appears that the actin-binding region contributes to the fast movement of Chara myosin XI. Mutation experiments of actin-binding surface loops support this hypothesis.
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Discovery of ultrafast myosin, its amino acid sequence, and structural features.,Haraguchi T, Tamanaha M, Suzuki K, Yoshimura K, Imi T, Tominaga M, Sakayama H, Nishiyama T, Murata T, Ito K Proc Natl Acad Sci U S A. 2022 Feb 22;119(8). pii: 2120962119. doi:, 10.1073/pnas.2120962119. PMID:35173046<ref>PMID:35173046</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7dhw" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Haraguchi, T]]
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[[Category: Haraguchi T]]
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[[Category: Imi, T]]
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[[Category: Imi T]]
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[[Category: Ito, K]]
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[[Category: Ito K]]
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[[Category: Murata, T]]
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[[Category: Murata T]]
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[[Category: Nishiyama, T]]
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[[Category: Nishiyama T]]
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[[Category: Sakayama, H]]
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[[Category: Sakayama H]]
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[[Category: Suzuki, K]]
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[[Category: Suzuki K]]
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[[Category: Tamanaha, M]]
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[[Category: Tamanaha M]]
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[[Category: Tominaga, M]]
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[[Category: Tominaga M]]
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[[Category: Yoshimura, K]]
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[[Category: Yoshimura K]]
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[[Category: Atp binding]]
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[[Category: Atpase]]
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[[Category: Motor domain]]
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[[Category: Motor protein]]
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[[Category: Myosin]]
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Current revision

Crystal structure of myosin-XI motor domain in complex with ADP-ALF4

PDB ID 7dhw

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