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4B3W

Crystal structure of human cytoglobin H(E7)Q mutant

4B3W の概要
エントリーDOI10.2210/pdb4b3w/pdb
関連するPDBエントリー1UMO 1URV 1URY 1UT0 1UX9 1V5H 2DC3
分子名称CYTOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (6 entities in total)
機能のキーワードoxygen transport, metal binding protein, heme hexacoordination, protein cavity
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Cytoplasm (By similarity): Q8WWM9
タンパク質・核酸の鎖数2
化学式量合計44550.88
構造登録者
主引用文献Gabba, M.,Abbruzzetti, S.,Spyrakis, F.,Forti, F.,Bruno, S.,Mozzarelli, A.,Luque, F.J.,Viappiani, C.,Cozzini, P.,Nardini, M.,Germani, F.,Bolognesi, M.,Moens, L.,Dewilde, S.
Co Rebinding Kinetics and Molecular Dynamics Simulations Highlight Dynamic Regulation of Internal Cavities in Human Cytoglobin.
Plos One, 8:49770-, 2013
Cited by
PubMed Abstract: Cytoglobin (Cygb) was recently discovered in the human genome and localized in different tissues. It was suggested to play tissue-specific protective roles, spanning from scavenging of reactive oxygen species in neurons to supplying oxygen to enzymes in fibroblasts. To shed light on the functioning of such versatile machinery, we have studied the processes supporting transport of gaseous heme ligands in Cygb. Carbon monoxide rebinding shows a complex kinetic pattern with several distinct reaction intermediates, reflecting rebinding from temporary docking sites, second order recombination, and formation (and dissociation) of a bis-histidyl heme hexacoordinated reaction intermediate. Ligand exit to the solvent occurs through distinct pathways, some of which exploit temporary docking sites. The remarkable change in energetic barriers, linked to heme bis-histidyl hexacoordination by HisE7, may be responsible for active regulation of the flux of reactants and products to and from the reaction site on the distal side of the heme. A substantial change in both protein dynamics and inner cavities is observed upon transition from the CO-liganded to the pentacoordinated and bis-histidyl hexacoordinated species, which could be exploited as a signalling state. These findings are consistent with the expected versatility of the molecular activity of this protein.
PubMed: 23308092
DOI: 10.1371/JOURNAL.PONE.0049770
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 4b3w
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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