Summary for 4ITR
| Entry DOI | 10.2210/pdb4itr/pdb |
| Descriptor | Adenosine monophosphate-protein transferase and cysteine protease IbpA, Cell division control protein 42 homolog, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | fic domain, adenosine monophosphate-protein transferase, transferase |
| Biological source | Haemophilus somnus More |
| Cellular location | Secreted. Protein p76 IgBP: Cell outer membrane; Peripheral membrane protein; Extracellular side (Probable): Q06277 Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P60953 |
| Total number of polymer chains | 4 |
| Total formula weight | 115568.67 |
| Authors | Xiao, J.,Dixon, J.E. (deposition date: 2013-01-18, release date: 2013-02-20, Last modification date: 2024-11-06) |
| Primary citation | Xiao, J.,Worby, C.A.,Mattoo, S.,Sankaran, B.,Dixon, J.E. Structural basis of Fic-mediated adenylylation. Nat.Struct.Mol.Biol., 17:1004-1010, 2010 Cited by PubMed Abstract: The Fic family of adenylyltransferases, defined by a core HPFx(D/E)GN(G/K)R motif, consists of over 2,700 proteins found in organisms from bacteria to humans. The immunoglobulin-binding protein A (IbpA) from the bacterial pathogen Histophilus somni contains two Fic domains that adenylylate the switch1 tyrosine residue of Rho-family GTPases, allowing the bacteria to subvert host defenses. Here we present the structure of the second Fic domain of IbpA (IbpAFic2) in complex with its substrate, Cdc42. IbpAFic2-bound Cdc42 mimics the GDI-bound state of Rho GTPases, with both its switch1 and switch2 regions gripped by IbpAFic2. Mutations disrupting the IbpAFic2-Cdc42 interface impair adenylylation and cytotoxicity. Notably, the switch1 tyrosine of Cdc42 is adenylylated in the structure, providing the first structural view for this post-translational modification. We also show that the nucleotide-binding mechanism is conserved among Fic proteins and propose a catalytic mechanism for this recently discovered family of enzymes. PubMed: 20622875DOI: 10.1038/nsmb.1867 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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