4MAX
Crystal structure of Synechococcus sp. PCC 7002 globin at cryogenic temperature with heme modification
Replaces: 4I0VSummary for 4MAX
Entry DOI | 10.2210/pdb4max/pdb |
Related | 1RTX 2KSC 4L2M |
Descriptor | cyanoglobin, HEME B/C, SULFATE ION, ... (4 entities in total) |
Functional Keywords | hemeprotein, 2/2 hemoglobin, glbn, trhbn, 2/2 globin, ros/rns detoxification, unknown function |
Biological source | Synechococcus sp. |
Total number of polymer chains | 3 |
Total formula weight | 43851.27 |
Authors | Wenke, B.B.,Schlessman, J.L.,Heroux, A.,Lecomte, J.T.J. (deposition date: 2013-08-18, release date: 2013-08-28, Last modification date: 2024-10-30) |
Primary citation | Wenke, B.B.,Lecomte, J.T.,Heroux, A.,Schlessman, J.L. The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures. Proteins, 82:528-534, 2014 Cited by PubMed Abstract: The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 Å resolution) and cyanide-bound (2.25 Å resolution) states with covalently attached heme. The two structures illustrate the conformational changes and cavity opening caused by exogenous ligand binding. They also reveal an unusually distorted heme, ruffled as in c cytochromes. Comparison to the solution structure demonstrates the influence of crystal packing on several structural elements, whereas comparison to GlbN from Synechocystis sp. PCC 6803 shows subtle differences in heme geometries and environment. The new structures will be instrumental in elucidating GlbN reactivity. PubMed: 23999883DOI: 10.1002/prot.24409 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.444 Å) |
Structure validation
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