2DGJ
Crystal structure of EbhA (756-1003 domain) from Staphylococcus aureus
Summary for 2DGJ
| Entry DOI | 10.2210/pdb2dgj/pdb |
| Related | 1xvh |
| Descriptor | hypothetical protein ebhA, SULFATE ION, ACETIC ACID, ... (5 entities in total) |
| Functional Keywords | helix-bundle, rod-like structure, adhesin, cell adhesion |
| Biological source | Staphylococcus aureus |
| Cellular location | Cell membrane; Single-pass membrane protein (Potential): Q931R6 |
| Total number of polymer chains | 2 |
| Total formula weight | 55453.72 |
| Authors | Tanaka, Y.,Yao, M.,Kuroda, M.,Watanabe, N.,Ohta, T.,Tanaka, I. (deposition date: 2006-03-14, release date: 2007-03-20, Last modification date: 2024-10-23) |
| Primary citation | Tanaka, Y.,Sakamoto, S.,Kuroda, M.,Goda, S.,Gao, Y.-G.,Tsumoto, K.,Hiragi, Y.,Yao, M.,Watanabe, N.,Ohta, T.,Tanaka, I. A helical string of alternately connected three-helix bundles for the cell wall-associated adhesion protein Ebh from Staphylococcus aureus Structure, 16:488-496, 2008 Cited by PubMed Abstract: The 1.1 MDa cell-wall-associated adhesion protein of staphylococci, Ebh, consists of several distinct regions, including a large central region with 52 imperfect repeats of 126 amino acid residues. We investigated the structure of this giant molecule by X-ray crystallography, circular dichroism (CD) spectrometry, and small-angle X-ray scattering (SAXS). The crystal structure of two repeats showed that each repeat consists of two distinct three-helix bundles, and two such repeats are connected along the long axis, resulting in a rod-like structure that is 120 A in length. CD and SAXS analyses of the samples with longer repeats suggested that each repeat has an identical structure, and that such repeats are connected tandemly to form a rod-like structure in solution, the length of which increased proportionately with the number of repeating units. On the basis of these results, it was proposed that Ebh is a 320 nm rod-like molecule with some plasticity at module junctions. PubMed: 18334223DOI: 10.1016/j.str.2007.12.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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