1LA6
The crystal structure of Trematomus newnesi hemoglobin in a partial hemichrome state
1LA6 の概要
| エントリーDOI | 10.2210/pdb1la6/pdb |
| 関連するPDBエントリー | 1T1N |
| 分子名称 | Hemoglobin alpha-1 chain, Hemoglobin beta-1/2 chain, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| 機能のキーワード | hemichrome, bishistidine complex, oxygen storage-transport complex, oxygen storage/transport |
| 由来する生物種 | Trematomus newnesi (dusky notothen) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 33210.69 |
| 構造登録者 | Riccio, A.,Vitagliano, L.,di Prisco, G.,Zagari, A.,Mazzarella, L. (登録日: 2002-03-28, 公開日: 2002-07-31, 最終更新日: 2024-11-20) |
| 主引用文献 | Riccio, A.,Vitagliano, L.,di Prisco, G.,Zagari, A.,Mazzarella, L. The crystal structure of a tetrameric hemoglobin in a partial hemichrome state Proc.Natl.Acad.Sci.USA, 99:9801-9806, 2002 Cited by PubMed Abstract: Tetrameric hemoglobins are the most widely used systems in studying protein cooperativity. Allosteric effects in hemoglobins arise from the switch between a relaxed (R) state and a tense (T) state occurring upon oxygen release. Here we report the 2.0-A crystal structure of the main hemoglobin component of the Antarctic fish Trematomus newnesi, in a partial hemichrome form. The two alpha-subunit iron atoms are bound to a CO molecule, whereas in the beta subunits the distal histidine residue is the sixth ligand of the heme iron. This structure, a tetrameric hemoglobin in the hemichrome state, demonstrates that the iron coordination by the distal histidine, usually associated with denaturing states, may be tolerated in a native-like hemoglobin structure. In addition, several features of the tertiary and quaternary organization of this structure are intermediate between the R and T states and agree well with the R --> T transition state properties obtained by spectroscopic and kinetic techniques. The analysis of this structure provides a detailed pathway of heme-heme communication and it indicates that the plasticity of the beta heme pocket plays a role in the R --> T transition of tetrameric hemoglobins. PubMed: 12093902DOI: 10.1073/pnas.132182099 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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