3MPB
Z5688 from E. coli O157:H7 bound to fructose
Summary for 3MPB
| Entry DOI | 10.2210/pdb3mpb/pdb |
| Related | 3KMH |
| Descriptor | Sugar isomerase, MANGANESE (II) ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | cupin, beta barrel, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, isomerase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 56404.43 |
| Authors | van Staalduinen, L.M.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2010-04-26, release date: 2010-07-21, Last modification date: 2024-11-27) |
| Primary citation | van Staalduinen, L.M.,Park, C.S.,Yeom, S.J.,Adams-Cioaba, M.A.,Oh, D.K.,Jia, Z. Structure-based annotation of a novel sugar isomerase from the pathogenic E. coli O157:H7. J.Mol.Biol., 401:866-881, 2010 Cited by PubMed Abstract: Prokaryotes can use a variety of sugars as carbon sources in order to provide a selective survival advantage. The gene z5688 found in the pathogenic Escherichia coli O157:H7 encodes a "hypothetical" protein of unknown function. Sequence analysis identified the gene product as a putative member of the cupin superfamily of proteins, but no other functional information was known. We have determined the crystal structure of the Z5688 protein at 1.6 A resolution and identified the protein as a novel E. coli sugar isomerase (EcSI) through overall fold analysis and secondary-structure matching. Extensive substrate screening revealed that EcSI is capable of acting on d-lyxose and d-mannose. The complex structure of EcSI with fructose allowed the identification of key active-site residues, and mutagenesis confirmed their importance. The structure of EcSI also suggested a novel mechanism for substrate binding and product release in a cupin sugar isomerase. Supplementation of a nonpathogenic E. coli strain with EcSI enabled cell growth on the rare pentose d-lyxose. PubMed: 20615418DOI: 10.1016/j.jmb.2010.06.063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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