2hf6: Difference between revisions

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==Solution structure of human zeta-COP==
==Solution structure of human zeta-COP==
<StructureSection load='2hf6' size='340' side='right'caption='[[2hf6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2hf6' size='340' side='right'caption='[[2hf6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HF6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2hf6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HF6 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COPZ1, COPZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2hf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf6 OCA], [https://pdbe.org/2hf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hf6 RCSB], [https://www.ebi.ac.uk/pdbsum/2hf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hf6 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=2hf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf6 OCA], [https://pdbe.org/2hf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hf6 RCSB], [https://www.ebi.ac.uk/pdbsum/2hf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hf6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/COPZ1_HUMAN COPZ1_HUMAN]] 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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).  The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.  
[https://www.uniprot.org/uniprot/COPZ1_HUMAN COPZ1_HUMAN] 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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).  The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hf6 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hf6 ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
COP-I-coated vesicles are protein and lipid carriers that mediate intra-Golgi transport and transport from the cis-Golgi complex to the endoplasmic reticulum in cells. The coatomer of the vesicles coat is comprised of seven subunits: alpha-COP, epsilon-COP, beta'-COP, beta-COP, gamma-COP, delta-COP, and zeta-COP. Here we report the solution structure of a truncated form (residues 1-149; zeta-COP149) of human zeta-COP (total 177 residues). It is the first three-dimensional structure of a "core" subunit of the COP I F-subcomplex. The structure of zeta-COP149 mainly consists of a disordered N-terminal tail, a five-stranded antiparallel beta-sheet, a two-stranded antiparallel beta-sheet, and five alpha-helices. The global folding of zeta-COP149 is very similar to the crystal structures of AP1-sigma1 and AP2-sigma2, directly demonstrating the structural similarity between the "core" subunits of the COP I F-subcomplex and adaptor protein complexes. Through structural comparison and mutagenesis study, we have also demonstrated that the heterodimers of zeta-COP149 and gamma-COP have packing interfaces and relative subunit orientations similar to those of AP2-sigma2 and AP2-alpha heterodimers. These results provide direct evidence supporting the previous proposal that the COP I F-subcomplex and adaptor protein complexes have similar tertiary and quaternary structures.


Solution structure of human zeta-COP: direct evidences for structural similarity between COP I and clathrin-adaptor coats.,Yu W, Lin J, Jin C, Xia B J Mol Biol. 2009 Mar 6;386(4):903-12. Epub 2009 Jan 10. PMID:19167404<ref>PMID:19167404</ref>
==See Also==
 
*[[Coatomer 3D structures|Coatomer 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hf6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Jin, C]]
[[Category: Jin C]]
[[Category: Xia, B]]
[[Category: Xia B]]
[[Category: Yu, W]]
[[Category: Yu W]]
[[Category: Cop i]]
[[Category: Protein transport]]

Latest revision as of 09:40, 1 May 2024

Solution structure of human zeta-COPSolution structure of human zeta-COP

Structural highlights

2hf6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COPZ1_HUMAN 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. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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