3TA8
Crystal structure HP-NAP from strain YS39 iron loaded (cocrystallization 5mM)
Summary for 3TA8
Entry DOI | 10.2210/pdb3ta8/pdb |
Related | 3T9J |
Descriptor | Neutrophil-activating protein, FE (III) ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | dodecamer, four-helix bundle, metal transport |
Biological source | Helicobacter pylori |
Total number of polymer chains | 1 |
Total formula weight | 19366.58 |
Authors | Tsuruta, O.,Yokoyama, H.,Fujii, S. (deposition date: 2011-08-03, release date: 2012-02-08, Last modification date: 2023-11-01) |
Primary citation | Tsuruta, O.,Yokoyama, H.,Fujii, S. A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP) Acta Crystallogr.,Sect.F, 68:134-140, 2012 Cited by PubMed Abstract: A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP) has been determined in two forms: the native state (Apo) at 2.20 Å resolution and an iron-loaded form (Fe-load) at 2.50 Å resolution. The highly solvated packing of the dodecameric shell is suitable for crystallographic study of the metal ion-uptake pathway. Like other bacterioferritins, HP-NAP forms a spherical dodecamer with 23 symmetry including two kinds of channels. Iron loading causes a series of conformational changes of amino-acid residues (Trp26, Asp52 and Glu56) at the ferroxidase centre. PubMed: 22297984DOI: 10.1107/S1744309111052675 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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