6BME
Crystal structure of Chlamydomonas reinhardtii THB4
Summary for 6BME
Entry DOI | 10.2210/pdb6bme/pdb |
Descriptor | Truncated hemoglobin 4, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total) |
Functional Keywords | globin, heme, truncated hemoglobin, 2-on-2 hemoglobin, lysine axial ligand, hexacoordinate, heme binding protein |
Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
Total number of polymer chains | 2 |
Total formula weight | 29511.47 |
Authors | Russo, M.M.,Schlessman, J.L.,Lecomte, J.T.J. (deposition date: 2017-11-14, release date: 2017-12-20, Last modification date: 2024-03-13) |
Primary citation | Johnson, E.A.,Russo, M.M.,Nye, D.B.,Schlessman, J.L.,Lecomte, J.T.J. Lysine as a heme iron ligand: A property common to three truncated hemoglobins from Chlamydomonas reinhardtii. Biochim Biophys Acta Gen Subj, 1862:2660-2673, 2018 Cited by PubMed Abstract: The nuclear genome of Chlamydomonas reinhardtii encodes a dozen hemoglobins of the truncated lineage. Four of these, named THB1-4, contain a single ~130-residue globin unit. THB1, which is cytoplasmic and capable of nitric oxide dioxygenation activity, uses a histidine and a lysine as axial ligands to the heme iron. In the present report, we compared THB2, THB3, and THB4 to THB1 to gain structural and functional insights into algal globins. PubMed: 30251657DOI: 10.1016/j.bbagen.2018.08.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.899 Å) |
Structure validation
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