3IB8

Crystal structure of full length Rv0805 in complex with 5'-AMP

3IB8 の概要

• エントリーDOI: 10.2210/pdb3ib8/pdb
• 関連するPDBエントリー: 2HY1 2HYO 2HYP 3IB7
• 分子名称: Icc protein, FE (III) ION, MANGANESE (II) ION, ... (8 entities in total)
• 機能のキーワード: metallophosphoesterase, alpha-beta fold, swapped-dimer, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36607.18

構造登録者

Podobnik, M.,Dermol, U. (登録日: 2009-07-15, 公開日: 2009-09-29, 最終更新日: 2023-11-01)

主引用文献

Podobnik, M.,Tyagi, R.,Matange, N.,Dermol, U.,Gupta, A.K.,Mattoo, R.,Seshadri, K.,Visweswariah, S.S.
A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability
J.Biol.Chem., 284:32846-32857, 2009

PubMed Abstract: Mycobacterium tuberculosis utilizes many mechanisms to establish itself within the macrophage, and bacterially derived cAMP is important in modulating the host cellular response. Although the genome of M. tuberculosis is endowed with a number of mammalian-like adenylyl cyclases, only a single cAMP phosphodiesterase has been identified that can decrease levels of cAMP produced by the bacterium. We present the crystal structure of the full-length and sole cAMP phosphodiesterase, Rv0805, found in M. tuberculosis, whose orthologs are present only in the genomes of slow growing and pathogenic mycobacteria. The dimeric core catalytic domain of Rv0805 adopts a metallophosphoesterase-fold, and the C-terminal region builds the active site and contributes to multiple substrate utilization. Localization of Rv0805 to the cell wall is dependent on its C terminus, and expression of either wild type or mutationally inactivated Rv0805 in M. smegmatis alters cell permeability to hydrophobic cytotoxic compounds. Rv0805 may therefore play a key role in the pathogenicity of mycobacteria, not only by hydrolyzing bacterial cAMP, but also by moonlighting as a protein that can alter cell wall functioning.

PubMed: 19801656
DOI: 10.1074/jbc.M109.049635

実験手法

X-RAY DIFFRACTION (1.8 Å)