3U35
Crystal structure of the general stress FMN/FAD binding protein from the phytopathogen Xanthomonas citri
Summary for 3U35
| Entry DOI | 10.2210/pdb3u35/pdb |
| Related | 1FLM 2I02 2OU5 3DMB 3U34 |
| Descriptor | General stress protein, TRIETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | xanthomonas citri general stress protein fmn binding protein fad binding protein, pnp-oxidase like fold, fmn/fad, protein binding |
| Biological source | Xanthomonas axonopodis pv. citri (Citrus canker) |
| Total number of polymer chains | 4 |
| Total formula weight | 80735.98 |
| Authors | Hilario, E.,Li, Y.,Fan, L. (deposition date: 2011-10-04, release date: 2012-06-27, Last modification date: 2024-02-28) |
| Primary citation | Hilario, E.,Li, Y.,Niks, D.,Fan, L. The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding property. Acta Crystallogr.,Sect.D, 68:846-853, 2012 Cited by PubMed Abstract: Xanthomonas citri pv. citri (Xac) causes citrus canker and affects citrus agriculture worldwide. Functional genetic analysis has indicated that a putative general stress protein (XacGSP) encoded by the Xac2369 gene is involved in the bacterial infection. In this report, the crystal structure of XacGSP was determined to 2.5 Å resolution. There are four XacGSP molecules in the crystal asymmetric unit. Each XacGSP monomer folds into a six-stranded antiparallel β-barrel flanked by five α-helices. A C-terminal extension protrudes from the sixth β-strand of the β-barrel and pairs with its counterpart from another monomer to form a bridge between the two subunits of an XacGSP dimer. Two XacGSP dimers cross over each other to form a tetramer; the β-barrels from one dimer contact the β-barrels of the other, while the two bridges are distant from each other and do not make contacts. The three-dimensional structure of the XacGSP monomer is very similar to those of pyridoxine 5-phosphate oxidases, a group of enzymes that use flavin mononucleotide (FMN) as a cofactor. Consistent with this, purified XacGSP protein binds to both FMN and flavin adenine dinucleotide (FAD), suggesting that XacGSP may help the bacteria to react against the oxidative stress induced by the defense mechanisms of the plant. PubMed: 22751670DOI: 10.1107/S0907444912014126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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