2BZT
NMR structure of the bacterial protein YFHJ from E. coli
Summary for 2BZT
| Entry DOI | 10.2210/pdb2bzt/pdb |
| NMR Information | BMRB: 6776 |
| Descriptor | PROTEIN ISCX (1 entity in total) |
| Functional Keywords | iron binding protein, iron sulphur clusters, isc operon, isc proteins |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 7737.53 |
| Authors | Pastore, C.,Kelly, G.,Adinolfi, S.,Mc Cormick, J.E.,Pastore, A. (deposition date: 2005-08-22, release date: 2006-12-06, Last modification date: 2024-05-15) |
| Primary citation | Pastore, C.,Adinolfi, S.,Huynen, M.A.,Rybin, V.,Martin, S.,Mayer, M.,Bukau, B.,Pastore, A. YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? Structure, 14:857-867, 2006 Cited by PubMed Abstract: The yfhJ gene is part of the isc operon, which encodes the machinery devoted to assemble iron-sulfur clusters in prokaryotes. Its transcript is a small acidic protein that binds the desulfurase IscS, which is essential in iron-specific metabolic pathways. To understand its cellular role, we have characterized the structure of YfhJ in solution and its interactions with potential cellular partners. It contains a modified winged helix motif, usually present in DNA binding proteins, and is able to bind iron cations. The IscS interaction surface is the same as that involved in iron binding. This observation and the pattern of conservation through species strongly suggest that YfhJ is a molecular adaptor that is able to modulate the function of IscS in iron-sulfur cluster formation. The remarkable similarity between the in vitro behavior of YfhJ and that of the protein frataxin also suggests new hypotheses regarding the functional role of both proteins. PubMed: 16698547DOI: 10.1016/j.str.2006.02.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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