4rv0: Difference between revisions

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'''Unreleased structure'''


The entry 4rv0 is ON HOLD  until Paper Publication
==Crystal structure of TN complex==
<StructureSection load='4rv0' size='340' side='right'caption='[[4rv0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rv0]] is a 8 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=4RV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.998&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4rv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv0 OCA], [https://pdbe.org/4rv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv0 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TERA_DROME TERA_DROME] Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/or anchoring during oogenesis. Involved in germ cell formation.<ref>PMID:14657277</ref> <ref>PMID:18590813</ref>


Authors: Hao, Q., Jiao, S., Shi, Z.B., Zhou, Z.C.
==See Also==
 
*[[ATPase 3D structures|ATPase 3D structures]]
Description: Crystal structure of TN complex
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Zhou, Z.C]]
__TOC__
[[Category: Hao, Q]]
</StructureSection>
[[Category: Jiao, S]]
[[Category: Drosophila melanogaster]]
[[Category: Shi, Z.B]]
[[Category: Large Structures]]
[[Category: Hao Q]]
[[Category: Jiao S]]
[[Category: Shi ZB]]
[[Category: Zhou ZC]]

Latest revision as of 13:30, 30 October 2024

Crystal structure of TN complexCrystal structure of TN complex

Structural highlights

4rv0 is a 8 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.998Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TERA_DROME Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/or anchoring during oogenesis. Involved in germ cell formation.[1] [2]

See Also

References

  1. ↑ Wojcik C, Yano M, DeMartino GN. RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis. J Cell Sci. 2004 Jan 15;117(Pt 2):281-92. Epub 2003 Dec 2. PMID:14657277 doi:http://dx.doi.org/10.1242/jcs.00841
  2. ↑ Thomson T, Liu N, Arkov A, Lehmann R, Lasko P. Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins. Mech Dev. 2008 Sep-Oct;125(9-10):865-73. doi: 10.1016/j.mod.2008.06.005. Epub, 2008 Jun 12. PMID:18590813 doi:http://dx.doi.org/10.1016/j.mod.2008.06.005

4rv0, resolution 2.00Å

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