4o2w: Difference between revisions

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'''Unreleased structure'''


The entry 4o2w is ON HOLD
==Crystal structure of the third RCC1-like domain of HERC1==
<StructureSection load='4o2w' size='340' side='right'caption='[[4o2w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4o2w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O2W 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=4o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o2w OCA], [https://pdbe.org/4o2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o2w RCSB], [https://www.ebi.ac.uk/pdbsum/4o2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o2w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HERC1_HUMAN HERC1_HUMAN] Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.<ref>PMID:8861955</ref> <ref>PMID:9233772</ref> <ref>PMID:15642342</ref>


Authors: Dong, A., Hu, J., Li, Y., Walker, J.R., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Tong, Y., Structural Genomics Consortium (SGC)
==See Also==
 
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
Description: Crystal structure of the third RCC1-like domain of HERC1
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Dong A]]
[[Category: Edwards AM]]
[[Category: Hu J]]
[[Category: Li Y]]
[[Category: Tong Y]]
[[Category: Walker JR]]

Latest revision as of 20:06, 20 September 2023

Crystal structure of the third RCC1-like domain of HERC1Crystal structure of the third RCC1-like domain of HERC1

Structural highlights

4o2w is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HERC1_HUMAN Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol 4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.[1] [2] [3]

See Also

References

  1. ↑ Rosa JL, Casaroli-Marano RP, Buckler AJ, Vilaro S, Barbacid M. p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 1996 Aug 15;15(16):4262-73. PMID:8861955
  2. ↑ Rosa JL, Barbacid M. A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70. Oncogene. 1997 Jul 3;15(1):1-6. PMID:9233772 doi:http://dx.doi.org/10.1038/sj.onc.1201170
  3. ↑ Garcia-Gonzalo FR, Bartrons R, Ventura F, Rosa JL. Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated guanine nucleotide release from ARF proteins. FEBS Lett. 2005 Jan 17;579(2):343-8. PMID:15642342 doi:http://dx.doi.org/S0014-5793(04)01504-2

4o2w, resolution 2.00Å

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