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| | <StructureSection load='6l4p' size='340' side='right'caption='[[6l4p]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6l4p' size='340' side='right'caption='[[6l4p]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6l4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L4P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6l4p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L4P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.703Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LC1, CHLREDRAFT_186669 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE]), ODA2, CHLREDRAFT_155136 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=6l4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l4p OCA], [http://pdbe.org/6l4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l4p RCSB], [http://www.ebi.ac.uk/pdbsum/6l4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l4p 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=6l4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l4p OCA], [https://pdbe.org/6l4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l4p RCSB], [https://www.ebi.ac.uk/pdbsum/6l4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l4p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNAL1_CHLRE DNAL1_CHLRE]] Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.<ref>PMID:10353837</ref> | + | [https://www.uniprot.org/uniprot/DNAL1_CHLRE DNAL1_CHLRE] Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.<ref>PMID:10353837</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 6l4p" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6l4p" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dynein 3D structures|Dynein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kurisu, G]] | + | [[Category: Kurisu G]] |
| - | [[Category: Nishikawa, Y]] | + | [[Category: Nishikawa Y]] |
| - | [[Category: Tanaka, H]] | + | [[Category: Tanaka H]] |
| - | [[Category: Toda, A]] | + | [[Category: Toda A]] |
| - | [[Category: Yagi, T]] | + | [[Category: Yagi T]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Contractile protein-motor protein complex]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| Structural highlights
Function
DNAL1_CHLRE Associates with the gamma heavy chain in the outer arm dynein. May target p45 polypeptide (an 45 kDa axonemal component) to the motor domain of the gamma heavy chain dynein.[1]
Publication Abstract from PubMed
Axonemal dynein is a microtubule-based molecular motor that drives ciliary/flagellar beating in eukaryotes. In axonemal dynein, the outer arm dynein (OAD) complex, which comprises three heavy chains (alpha, beta, and gamma), produces the main driving force for ciliary/flagellar motility. It has recently been shown that axonemal dynein light chain-1 (LC1) binds to the microtubule-binding domain (MTBD) of OADgamma, leading to a decrease in its microtubule-binding affinity. However, it remains unclear how LC1 interacts with the MTBD and controls the microtubule-binding affinity of OADgamma. Here, we have used X-ray crystallography and pull-down assays to examine the interaction between LC1 and the MTBD, identifying two important sites of interaction in the MTBD. Solving the LC1-MTBD complex from Chlamydomonas reinhardtii at 1.7 A resolution, we observed that one site is located in the H5 helix and that the other is located in the flap region that is unique to some axonemal dynein MTBDs. Mutational analysis of key residues in these sites indicated that the H5 helix is the main LC1-binding site. We modeled the ternary structure of the LC1-MTBD complex bound to microtubules based on the known dynein-microtubule complex. This enabled us to propose a structural basis for both formations of the ternary LC1-MTBD-microtubule complex and LC1-mediated tuning of MTBD binding to the microtubule, suggesting a molecular model for how axonemal dynein senses the curvature of the axoneme and tunes ciliary/flagellar beating.
The complex of outer-arm dynein light chain-1 and the microtubule-binding domain of the gamma heavy chain shows how axonemal dynein tunes ciliary beating.,Toda A, Nishikawa Y, Tanaka H, Yagi T, Kurisu G J Biol Chem. 2020 Feb 3. pii: RA119.011541. doi: 10.1074/jbc.RA119.011541. PMID:32014992[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benashski SE, Patel-King RS, King SM. Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the gamma heavy chain. Biochemistry. 1999 Jun 1;38(22):7253-64. PMID:10353837 doi:http://dx.doi.org/10.1021/bi990466y
- ↑ Toda A, Nishikawa Y, Tanaka H, Yagi T, Kurisu G. The complex of outer-arm dynein light chain-1 and the microtubule-binding domain of the gamma heavy chain shows how axonemal dynein tunes ciliary beating. J Biol Chem. 2020 Feb 3. pii: RA119.011541. doi: 10.1074/jbc.RA119.011541. PMID:32014992 doi:http://dx.doi.org/10.1074/jbc.RA119.011541
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