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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