3AT7
Crystal structure of bacterial cell-surface alginate-binding protein Algp7
Summary for 3AT7
| Entry DOI | 10.2210/pdb3at7/pdb |
| Descriptor | Alginate-binding flagellin (2 entities in total) |
| Functional Keywords | two up-and-down four-helical bundles, alginate binding, alginate, structural protein |
| Biological source | Sphingomonas |
| Total number of polymer chains | 2 |
| Total formula weight | 63402.18 |
| Authors | Maruyama, Y.,Ochiai, A.,Mikami, B.,Hashimoto, W.,Murata, K. (deposition date: 2010-12-27, release date: 2011-02-23, Last modification date: 2024-03-13) |
| Primary citation | Maruyama, Y.,Ochiai, A.,Mikami, B.,Hashimoto, W.,Murata, K. Crystal structure of bacterial cell-surface alginate-binding protein with an M75 peptidase motif. Biochem.Biophys.Res.Commun., 405:411-416, 2011 Cited by PubMed Abstract: A gram-negative Sphingomonas sp. A1 directly incorporates alginate polysaccharide into the cytoplasm via the cell-surface pit and ABC transporter. A cell-surface alginate-binding protein, Algp7, functions as a concentrator of the polysaccharide in the pit. Based on the primary structure and genetic organization in the bacterial genome, Algp7 was found to be homologous to an M75 peptidase motif-containing EfeO, a component of a ferrous ion transporter. Despite the presence of an M75 peptidase motif with high similarity, the Algp7 protein purified from recombinant Escherichia coli cells was inert on insulin B chain and N-benzoyl-Phe-Val-Arg-p-nitroanilide, both of which are substrates for a typical M75 peptidase, imelysin, from Pseudomonas aeruginosa. The X-ray crystallographic structure of Algp7 was determined at 2.10Å resolution by single-wavelength anomalous diffraction. Although a metal-binding motif, HxxE, conserved in zinc ion-dependent M75 peptidases is also found in Algp7, the crystal structure of Algp7 contains no metal even at the motif. The protein consists of two structurally similar up-and-down helical bundles as the basic scaffold. A deep cleft between the bundles is sufficiently large to accommodate macromolecules such as alginate polysaccharide. This is the first structural report on a bacterial cell-surface alginate-binding protein with an M75 peptidase motif. PubMed: 21238429DOI: 10.1016/j.bbrc.2011.01.043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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