4L2M

Crystal structure of the 2/2 hemoglobin from Synechococcus sp. PCC 7002 in the cyanomet state and with covalently attached heme

Summary for 4L2M

• Entry DOI: 10.2210/pdb4l2m/pdb
• Related: 1DLY 1RTX 1S69 2KSC 4I0V
• Descriptor: Cyanoglobin, HEME B/C, CYANIDE ION, ... (5 entities in total)
• Functional Keywords: group i 2/2 hemoglobin, glbn, trhbn, cyanomet hemoglobin, histidine-heme covalent linkage, truncated hemoglobin, unknown function
• Biological source: Synechococcus sp.
• Total number of polymer chains: 2
• Total formula weight: 29062.06

Authors

Wenke, B.B.,Schlessman, J.L.,Heroux, A.,Lecomte, J.T.J. (deposition date: 2013-06-04, release date: 2013-06-12, Last modification date: 2024-11-20)

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

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: 23999883
DOI: 10.1002/prot.24409

Experimental method

X-RAY DIFFRACTION (2.25 Å)