6fv0

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==Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA==
==Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA==
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<StructureSection load='6fv0' size='340' side='right' caption='[[6fv0]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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<StructureSection load='6fv0' size='340' side='right'caption='[[6fv0]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fv0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FV0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fv0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FV0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.29&#8491;</td></tr>
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<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=6fv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fv0 OCA], [http://pdbe.org/6fv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fv0 RCSB], [http://www.ebi.ac.uk/pdbsum/6fv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fv0 ProSAT]</span></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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fv0 OCA], [https://pdbe.org/6fv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fv0 RCSB], [https://www.ebi.ac.uk/pdbsum/6fv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fv0 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TOR1A_MOUSE TOR1A_MOUSE] Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues.<ref>PMID:16364897</ref> <ref>PMID:17200151</ref> <ref>PMID:17428918</ref> <ref>PMID:18827015</ref> <ref>PMID:20457914</ref> [https://www.uniprot.org/uniprot/KLC1_MOUSE KLC1_MOUSE] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.[UniProtKB:P37285]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat of kinesin light chain 2 in complex with a cargo peptide harboring a 'tryptophan-acidic' motif derived from SKIP, a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition.
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The light chains (KLCs) of the heterotetrameric microtubule motor kinesin-1, that bind to cargo adaptor proteins and regulate its activity, have a capacity to recognize short peptides via their tetratricopeptide repeat domains (KLC(TPR)). Here, using X-ray crystallography, we show how kinesin-1 recognizes a novel class of adaptor motifs that we call 'Y-acidic' (tyrosine flanked by acidic residues), in a KLC-isoform-specific manner. Binding specificities of Y-acidic motifs (present in JIP1 and in TorsinA) to KLC1(TPR) are distinct from those utilized for the recognition of W-acidic motifs, found in adaptors, that are KLC-isoform non-selective. However, a partial overlap on their receptor-binding sites implies that adaptors relying on Y-acidic and W-acidic motifs must act independently. We propose a model to explain why these two classes of motifs that bind to the concave surface of KLC(TPR) with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity.
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Structural Basis For Kinesin-1:Cargo Recognition.,Pernigo S, Lamprecht A, Steiner RA, Dodding MP Science. 2013 Mar 21. PMID:23519214<ref>PMID:23519214</ref>
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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors.,Pernigo S, Chegkazi MS, Yip YY, Treacy C, Glorani G, Hansen K, Politis A, Bui S, Dodding MP, Steiner RA Elife. 2018 Oct 15;7:e38362. doi: 10.7554/eLife.38362. PMID:30320553<ref>PMID:30320553</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 6fv0" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6fv0" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Kinesin 3D Structures|Kinesin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dodding, M P]]
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[[Category: Lama glama]]
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[[Category: Pernigo, S]]
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[[Category: Large Structures]]
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[[Category: Steiner, R A]]
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[[Category: Mus musculus]]
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[[Category: Cargo recognition]]
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[[Category: Dodding MP]]
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[[Category: Motor protein]]
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[[Category: Pernigo S]]
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[[Category: Nanobody]]
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[[Category: Steiner RA]]
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[[Category: Protein complex]]
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Current revision

Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA

PDB ID 6fv0

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