4KZS
Crystal structure of the secreted protein HP1454 from the human pathogen Helicobacter pylori
Summary for 4KZS
| Entry DOI | 10.2210/pdb4kzs/pdb |
| Descriptor | LPP20 lipofamily protein, PENTAETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | helicobacter pylori, secreted proteins, outer membrane, tol-pal system, three-helix bundle, unknown function |
| Biological source | Helicobacter pylori R046Wa |
| Total number of polymer chains | 1 |
| Total formula weight | 32257.59 |
| Authors | Quarantini, S.,Cendron, L.,Fischer, W.,Zanotti, G. (deposition date: 2013-05-30, release date: 2014-06-04, Last modification date: 2024-02-28) |
| Primary citation | Quarantini, S.,Cendron, L.,Zanotti, G. Crystal structure of the secreted protein HP1454 from the human pathogen Helicobacter pylori. Proteins, 82:2868-2873, 2014 Cited by PubMed Abstract: HP1454 is a protein of 303 amino acids found in the extracellular milieu of Helicobacter pylori. The protein structure, crystallized in the orthorhombic C222₁ space group with one molecule per asymmetric unit, has been determined using the single-wavelength anomalous dispersion method. HP1454 exhibits an elongated bent shape, composed of three distinct domains. Each domain possesses a fold already present in other structures: Domain I contains a three-strand antiparallel β-barrel flanked by a long α-helix, Domain II is an anti-parallel three-helix bundle, and Domain III a β-sheet flanked by two α-helices. The overall assembly of the protein does not bear any similarity with known structures. PubMed: 24854568DOI: 10.1002/prot.24608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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