|
|
Line 3: |
Line 3: |
| <SX load='6sct' size='340' side='right' viewer='molstar' caption='[[6sct]], [[Resolution|resolution]] 4.69Å' scene=''> | | <SX load='6sct' size='340' side='right' viewer='molstar' caption='[[6sct]], [[Resolution|resolution]] 4.69Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6sct]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6sbz 6sbz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sct]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCT FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG]), CLTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</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]] 4.69Å</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=6sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sct OCA], [http://pdbe.org/6sct PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sct RCSB], [http://www.ebi.ac.uk/pdbsum/6sct PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sct 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=6sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sct OCA], [https://pdbe.org/6sct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sct RCSB], [https://www.ebi.ac.uk/pdbsum/6sct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sct ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/C0MHR2_PIG C0MHR2_PIG]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[PIRNR:PIRNR002290] [[http://www.uniprot.org/uniprot/F1S398_PIG F1S398_PIG]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[RuleBase:RU363137] | + | [https://www.uniprot.org/uniprot/F1S398_PIG F1S398_PIG] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[RuleBase:RU363137] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
Line 18: |
Line 18: |
| </div> | | </div> |
| <div class="pdbe-citations 6sct" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6sct" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Clathrin 3D structures|Clathrin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
Line 23: |
Line 26: |
| </SX> | | </SX> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
- | [[Category: Cameron, A D]] | + | [[Category: Cameron AD]] |
- | [[Category: Morris, K L]] | + | [[Category: Morris KL]] |
- | [[Category: Sessions, R]] | + | [[Category: Sessions R]] |
- | [[Category: Smith, C J]] | + | [[Category: Smith CJ]] |
- | [[Category: Clathrin]]
| + | |
- | [[Category: Coat protein]]
| + | |
- | [[Category: Endocytosis]]
| + | |
- | [[Category: Trafficking]]
| + | |
- | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
F1S398_PIG Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.[RuleBase:RU363137]
Publication Abstract from PubMed
Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain-heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein-protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.
Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.,Morris KL, Jones JR, Halebian M, Wu S, Baker M, Armache JP, Avila Ibarra A, Sessions RB, Cameron AD, Cheng Y, Smith CJ Nat Struct Mol Biol. 2019 Oct;26(10):890-898. doi: 10.1038/s41594-019-0292-0., Epub 2019 Oct 3. PMID:31582853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morris KL, Jones JR, Halebian M, Wu S, Baker M, Armache JP, Avila Ibarra A, Sessions RB, Cameron AD, Cheng Y, Smith CJ. Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nat Struct Mol Biol. 2019 Oct;26(10):890-898. doi: 10.1038/s41594-019-0292-0., Epub 2019 Oct 3. PMID:31582853 doi:http://dx.doi.org/10.1038/s41594-019-0292-0
|