6VRI

Crystal Structure of the wtBlc-split Protein

6VRI の概要

• エントリーDOI: 10.2210/pdb6vri/pdb
• 分子名称: Outer membrane lipoprotein Blc, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: lipocalin, heme, beta barrel, split protein, unknown function
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 62374.28

構造登録者

Bozhanova, N.G.,Meiler, J. (登録日: 2020-02-07, 公開日: 2020-12-02, 最終更新日: 2023-10-11)

主引用文献

Bozhanova, N.G.,Calcutt, M.W.,Beavers, W.N.,Brown, B.P.,Skaar, E.P.,Meiler, J.
Lipocalin Blc is a potential heme-binding protein.
Febs Lett., 595:206-219, 2021

PubMed Abstract: Lipocalins are a superfamily of functionally diverse proteins defined by a well-conserved tertiary structure despite variation in sequence. Lipocalins bind and transport small hydrophobic molecules in organisms of all kingdoms. However, there is still uncertainty regarding the function of some members of the family, including bacterial lipocalin Blc from Escherichia coli. Here, we present evidence that lipocalin Blc may be involved in heme binding, trans-periplasmic transport, or heme storage. This conclusion is supported by a cocrystal structure, mass-spectrometric data, absorption titration, and in silico analysis. Binding of heme is observed at low micromolar range with one-to-one ligand-to-protein stoichiometry. However, the absence of classical coordination to the iron atom leaves the possibility that the primary ligand of Blc is another tetrapyrrole.

PubMed: 33210733
DOI: 10.1002/1873-3468.14001

実験手法

X-RAY DIFFRACTION (1.94 Å)