This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2ynp

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

yeast betaprime COP 1-604 with KTKTN motif

Structural highlights

2ynp is a 2 chain structure with sequence from Saccharomyces cerevisiae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.962Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COPB2_YEAST The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.^[1]

Publication Abstract from PubMed

COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD-repeat domain of beta'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the beta'-COP propeller. An absolute requirement of a two-residue spacing between the terminal carboxylate group and first lysine residue results from interactions of carbonyl groups in the motif backbone with basic side chains of beta'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous alpha-COP domain. Mutation of key interacting residues in either domain or in their cognate motifs abolishes in vitro binding and results in mistrafficking of dilysine-containing cargo in yeast without compromising cell viability. Flexibility between beta'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.

Molecular Basis for Recognition of Dilysine Trafficking Motifs by COPI.,Jackson LP, Lewis M, Kent HM, Edeling MA, Evans PR, Duden R, Owen DJ Dev Cell. 2012 Nov 20. pii: S1534-5807(12)00480-7. doi:, 10.1016/j.devcel.2012.10.017. PMID:23177648^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gabriely G, Kama R, Gerst JE. Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast. Mol Cell Biol. 2007 Jan;27(2):526-40. Epub 2006 Nov 13. PMID:17101773 doi:MCB.00577-06
↑ Jackson LP, Lewis M, Kent HM, Edeling MA, Evans PR, Duden R, Owen DJ. Molecular Basis for Recognition of Dilysine Trafficking Motifs by COPI. Dev Cell. 2012 Nov 20. pii: S1534-5807(12)00480-7. doi:, 10.1016/j.devcel.2012.10.017. PMID:23177648 doi:http://dx.doi.org/10.1016/j.devcel.2012.10.017

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ynp"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ynp' size='340' side='right'caption='[[2ynp]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ynp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ynp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNP FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ynn|2ynn]], [[2yno|2yno]]</div></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]] 2.962&#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=2ynp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ynp OCA], [https://pdbe.org/2ynp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ynp RCSB], [https://www.ebi.ac.uk/pdbsum/2ynp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ynp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/COPB2_YEAST COPB2_YEAST]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.<ref>PMID:17101773</ref>
+[https://www.uniprot.org/uniprot/COPB2_YEAST COPB2_YEAST] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.<ref>PMID:17101773</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Duden, R]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Edeling, M A]]
+[[Category: Synthetic construct]]
-[[Category: Evans, P R]]
+[[Category: Duden R]]
-[[Category: Jackson, L P]]
+[[Category: Edeling MA]]
-[[Category: Kent, H M]]
+[[Category: Evans PR]]
-[[Category: Lewis, M]]
+[[Category: Jackson LP]]
-[[Category: Owen, D J]]
+[[Category: Kent HM]]
-[[Category: Copi-mediated trafficking]]
+[[Category: Lewis M]]
-[[Category: Dilysine motif]]
+[[Category: Owen DJ]]
-[[Category: Membrane trafficking]]
-[[Category: Protein transport]]

2ynp

From Proteopedia

Current revision

yeast betaprime COP 1-604 with KTKTN motif

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox