6E4D

Atomic structure of Mycobacterium tuberculosis DppA

6E4D の概要

• エントリーDOI: 10.2210/pdb6e4d/pdb
• 関連するPDBエントリー: 6E3D
• 分子名称: Periplasmic dipeptide-binding lipoprotein DPPA, VAL-VAL-VAL-ALA (3 entities in total)
• 機能のキーワード: heme-binding, periplasmic protein, metal binding protein
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55783.95

構造登録者

Ko, Y.,Mitra, A.,Niederweis, M.,Cingolani, G. (登録日: 2018-07-17, 公開日: 2019-09-11, 最終更新日: 2023-10-11)

主引用文献

Mitra, A.,Ko, Y.H.,Cingolani, G.,Niederweis, M.
Heme and hemoglobin utilization by Mycobacterium tuberculosis.
Nat Commun, 10:4260-4260, 2019

PubMed Abstract: Iron is essential for growth of Mycobacterium tuberculosis (Mtb), but most iron in the human body is stored in heme within hemoglobin. Here, we demonstrate that the substrate-binding protein DppA of the inner membrane Dpp transporter is required for heme and hemoglobin utilization by Mtb. The 1.27 Å crystal structure of DppA shows a tetrapeptide bound in the protein core and a large solvent-exposed crevice for heme binding. Mutation of arginine 179 in this cleft eliminates heme binding to DppA and prevents heme utilization by Mtb. The outer membrane proteins PPE36 and PPE62 are also required for heme and hemoglobin utilization, indicating that these pathways converge at the cell surface of Mtb. Albumin, the most abundant blood protein, binds heme specifically and bypasses the requirements for PPE36, PPE62 and Dpp. Thus, our study reveals albumin-dependent and -independent heme uptake pathways, highlighting the importance of iron acquisition from heme for Mtb.

PubMed: 31534126
DOI: 10.1038/s41467-019-12109-5

実験手法

X-RAY DIFFRACTION (1.252 Å)