3VOL
X-ray Crystal Structure of PAS-HAMP Aer2 in the CN-bound Form
Summary for 3VOL
| Entry DOI | 10.2210/pdb3vol/pdb |
| Descriptor | Aerotaxis transducer Aer2, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (4 entities in total) |
| Functional Keywords | heme, oxygen sensor protein, pas, hamp, cyanomet, cn-bound, signaling protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 26442.43 |
| Authors | Sawai, H.,Sugimoto, H.,Shiro, Y.,Aono, S. (deposition date: 2012-01-27, release date: 2012-05-23, Last modification date: 2024-03-20) |
| Primary citation | Sawai, H.,Sugimoto, H.,Shiro, Y.,Ishikawa, H.,Mizutani, Y.,Aono, S. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa Chem.Commun.(Camb.), 48:6523-6525, 2012 Cited by PubMed Abstract: The crystal structure of a truncated Aer2, a signal transducer protein from Pseudomonas aeruginosa, consisting of the heme-containing PAS and di-HAMP domains revealed that a distal tryptophan residue (Trp283) plays an important role in stabilizing the heme-bound O(2) and intra-molecular signal transduction upon O(2) binding. PubMed: 22622145DOI: 10.1039/c2cc32549g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.399 Å) |
Structure validation
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