4XPY

Crystal structure of hemerythrin : L114Y mutant

4XPY の概要

• エントリーDOI: 10.2210/pdb4xpy/pdb
• 関連するPDBエントリー: 4xpw 4xpx 4xq1
• 分子名称: Bacteriohemerythrin, FE (II) ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: oxygen binding protein
• 由来する生物種: Methylococcus capsulatus str. Bath
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14990.47

構造登録者

Chuankhayan, P.,Chen, K.H.C.,Wu, H.H.,Chen, C.J.,Fukuda, M.,Yu, S.S.F.,Chan, S.I. (登録日: 2015-01-18, 公開日: 2015-04-29, 最終更新日: 2023-11-08)

主引用文献

Chen, K.H.C.,Chuankhayan, P.,Wu, H.H.,Chen, C.J.,Fukuda, M.,Yu, S.S.F.,Chan, S.I.
The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal that Leu114 regulates a water tunnel.
J.Inorg.Biochem., 150:81-89, 2015

PubMed Abstract: The bacteriohemerythrin (McHr) from Methylococcus capsulatus (Bath) is an oxygen carrier that serves as a transporter to deliver O2 from the cytosol of the bacterial cell body to the particulate methane monooxygenase residing in the intracytoplasmic membranes for methane oxidation. Here we report X-ray protein crystal structures of the recombinant wild type (WT) McHr and its L114A, L114Y and L114F mutants. The structure of the WT reveals a possible water tunnel in the McHr that might be linked to its faster autoxidation relative to hemerythrin in marine invertebrates. With Leu114 positioned at the end of this putative water tunnel, the hydrophobic side chain of this residue seems to play a prominent role in controlling the access of the water molecule required for autoxidation. This hypothesis is examined by comparing the autoxidation rates of the WT McHr with those of the L114A, L114Y and L114F mutants. The biochemical data are correlated with structural insights derived from the analysis of the putative water tunnels in the various McHr proteins provided by the X-ray structures.

PubMed: 25890483
DOI: 10.1016/j.jinorgbio.2015.04.001

実験手法

X-RAY DIFFRACTION (1.13 Å)