7bjg

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<StructureSection load='7bjg' size='340' side='right'caption='[[7bjg]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='7bjg' size='340' side='right'caption='[[7bjg]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7bjg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7bjg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJG FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tm1, 10, 1305, 2299, BcDNA:GH09289, BcDNA:LD37158, BcDNA:SD21996, chr3R:11122272..11122408, cTM, cTm, cTmII, Dm Tm1, Dm TmH33, Dm TmH34, Dmel\CG4898, DmTm1, l(3)02299, l(3)S130510, l(3)s2958, mTmII, PmI, region 3, TM, Tm, TM1, tm1, TmH, TmH-33, TmH-34, TmH33, TmH34, TMII, TmII, tmII, Tmr33, Tmr34, TnH, TnH-33, TnH-34, tropomyosin, CG4898, Dmel_CG4898 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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]] 2.45&#8491;</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=7bjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bjg OCA], [https://pdbe.org/7bjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bjg RCSB], [https://www.ebi.ac.uk/pdbsum/7bjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bjg 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=7bjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bjg OCA], [https://pdbe.org/7bjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bjg RCSB], [https://www.ebi.ac.uk/pdbsum/7bjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bjg ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8IGY1_DROME Q8IGY1_DROME]
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Kinesin-1 carries cargos including proteins, RNAs, vesicles, and pathogens over long distances within cells. The mechanochemical cycle of kinesins is well described, but how they establish cargo specificity is not fully understood. Transport of oskar mRNA to the posterior pole of the Drosophila oocyte is mediated by Drosophila kinesin-1, also called kinesin heavy chain (Khc), and a putative cargo adaptor, the atypical tropomyosin, aTm1. How the proteins cooperate in mRNA transport is unknown. Here, we present the high-resolution crystal structure of a Khc-aTm1 complex. The proteins form a tripartite coiled coil comprising two in-register Khc chains and one aTm1 chain, in antiparallel orientation. We show that aTm1 binds to an evolutionarily conserved cargo binding site on Khc, and mutational analysis confirms the importance of this interaction for mRNA transport in vivo. Furthermore, we demonstrate that Khc binds RNA directly and that it does so via its alternative cargo binding domain, which forms a positively charged joint surface with aTm1, as well as through its adjacent auxiliary microtubule binding domain. Finally, we show that aTm1 plays a stabilizing role in the interaction of Khc with RNA, which distinguishes aTm1 from classical motor adaptors.
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Molecular basis of mRNA transport by a kinesin-1-atypical tropomyosin complex.,Dimitrova-Paternoga L, Jagtap PKA, Cyrklaff A, Vaishali, Lapouge K, Sehr P, Perez K, Heber S, Low C, Hennig J, Ephrussi A Genes Dev. 2021 Jun 17. pii: gad.348443.121. doi: 10.1101/gad.348443.121. PMID:34140355<ref>PMID:34140355</ref>
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==See Also==
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*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
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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 7bjg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dimitrova-Paternoga, L]]
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[[Category: Dimitrova-Paternoga L]]
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[[Category: Ephrussi, A]]
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[[Category: Ephrussi A]]
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[[Category: Hennig, J]]
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[[Category: Hennig J]]
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[[Category: Jagtap, P K.A]]
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[[Category: Jagtap PKA]]
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[[Category: Binds khc]]
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[[Category: Coiled-coil]]
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[[Category: Drosophila oocyte]]
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[[Category: Rna transport]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of atypical Tm1 (Tm1-I/C), residues 262-363

PDB ID 7bjg

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