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6BME

Crystal structure of Chlamydomonas reinhardtii THB4

Summary for 6BME
Entry DOI10.2210/pdb6bme/pdb
DescriptorTruncated hemoglobin 4, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
Functional Keywordsglobin, heme, truncated hemoglobin, 2-on-2 hemoglobin, lysine axial ligand, hexacoordinate, heme binding protein
Biological sourceChlamydomonas reinhardtii (Chlamydomonas smithii)
Total number of polymer chains2
Total formula weight29511.47
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 citationJohnson, 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: 30251657
DOI: 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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