4L2M

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

4L2M の概要

• エントリーDOI: 10.2210/pdb4l2m/pdb
• 関連するPDBエントリー: 1DLY 1RTX 1S69 2KSC 4I0V
• 分子名称: Cyanoglobin, HEME B/C, CYANIDE ION, ... (5 entities in total)
• 機能のキーワード: group i 2/2 hemoglobin, glbn, trhbn, cyanomet hemoglobin, histidine-heme covalent linkage, truncated hemoglobin, unknown function
• 由来する生物種: Synechococcus sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29062.06

構造登録者

Wenke, B.B.,Schlessman, J.L.,Heroux, A.,Lecomte, J.T.J. (登録日: 2013-06-04, 公開日: 2013-06-12, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.25 Å)