3LZQ
Crystal Structure Analysis of Manganese treated P19 protein from Campylobacter jejuni at 1.41 A at pH 9
Summary for 3LZQ
| Entry DOI | 10.2210/pdb3lzq/pdb |
| Related | 2O6C 2O6D 2O6E 2O6F 3LZL 3LZN 3LZO 3LZP 3LZR |
| Descriptor | P19 protein, COPPER (II) ION, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | copper binding, iron transport, iron uptake, p19 delition, transport protein |
| Biological source | Campylobacter jejuni |
| Total number of polymer chains | 2 |
| Total formula weight | 35610.81 |
| Authors | Doukov, T.I.,Chan, A.C.K.,Scofield, M.,Ramin, A.B.,Tom-Yew, S.A.L.,Murphy, M.E.P. (deposition date: 2010-03-01, release date: 2010-07-21, Last modification date: 2024-04-03) |
| Primary citation | Chan, A.C.,Doukov, T.I.,Scofield, M.,Tom-Yew, S.A.,Ramin, A.B.,Mackichan, J.K.,Gaynor, E.C.,Murphy, M.E. Structure and Function of P19, a High-Affinity Iron Transporter of the Human Pathogen Campylobacter jejuni. J.Mol.Biol., 401:590-604, 2010 Cited by PubMed Abstract: Campylobacter jejuni, a major cause of acute bacterial diarrhea in humans, expresses numerous proteins to import diverse forms of essential iron. The expression of p19 and an adjacent iron transporter homologue (ftr1) is strongly induced upon iron limitation, suggesting a function in iron acquisition. Here, we show that the loss of P19 alone is detrimental to growth on iron-restricted media. Furthermore, metal binding analysis demonstrates that recombinant P19 has distinct copper and iron binding sites. Crystal structures of P19 have been solved to 1.41 A resolution, revealing an immunoglobulin-like fold. A P19 homodimer in which both monomers contribute ligands to two equivalent copper sites located adjacent to methionine-rich patches is observed. Copper coordination occurs via three histidine residues (His42, His95, and His132) and Met88. A solvent channel lined with conserved acidic residues leads to the copper site. Soaking crystals with a solution of manganese as iron analog reveals a second metal binding site in this solvent channel (metal-metal distance, 7.7 A). Glu44 lies between the metal sites and displays multiple conformations in the crystal structures, suggesting a role in regulating metal-metal interaction. Dimerization is shown to be metal dependent in vitro and is detected in vivo by cross-linking. PubMed: 20600116DOI: 10.1016/j.jmb.2010.06.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.41 Å) |
Structure validation
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