7W58

Crystal structure of acyl-carrier protein synthase from Mycobacterium smegmatis

7W58 の概要

• エントリーDOI: 10.2210/pdb7w58/pdb
• 分子名称: 4'-phosphopantetheinyl transferase, 1,2-ETHANEDIOL, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: acps, mycobacterium smegmatis, transferase
• 由来する生物種: Mycolicibacterium smegmatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14368.85

構造登録者

Yadav, S.,Bhatia, I.,Biswal, B.K. (登録日: 2021-11-29, 公開日: 2022-06-29, 最終更新日: 2023-11-29)

主引用文献

Bhatia, I.,Yadav, S.,Biswal, B.K.
Identification, structure determination and analysis of Mycobacterium smegmatis acyl-carrier protein synthase (AcpS) crystallized serendipitously.
Acta Crystallogr.,Sect.F, 78:252-264, 2022

PubMed Abstract: The unintended crystallization of proteins which generally originate from the expression host instead of the target recombinant proteins is periodically reported. Despite the massive technological advances in the field, assigning a structural model to the corresponding diffraction data is not a trivial task. Here, the structure of acyl-carrier protein synthase (AcpS) from Mycobacterium smegmatis (msAcpS), which crystallized inadvertently in an experimental setup to grow crystals of a Mycobacterium tuberculosis protein using M. smegmatis as an expression system, is reported. After numerous unsuccessful attempts to solve the structure of the target protein by the molecular-replacement method no convincing solutions were obtained, indicating that the diffraction data may correspond to a crystal of an artifactual protein, which was finally identified by the Sequence-Independent Molecular replacement Based on Available Databases (SIMBAD) server. The msAcpS structure was solved at 2.27 Å resolution and structural analysis showed an overall conserved fold. msAcpS formed a trimeric structure similar to those of other reported structures of AcpS from various organisms; however, the residues involved in trimer formation are not strictly conserved. An unrelated metal ion (Ni), which was possibly incorporated during protein purification, was observed in the proximity of His49 and His116. Structural and sequence differences were observed in the loop connecting the α3 and α4 helices that is responsible for the open and closed conformations of the enzyme. Moreover, the structural analysis of msAcpS augments the current understanding of this enzyme, which plays a crucial role in the functional activation of acyl-carrier proteins in the fatty-acid biosynthesis pathway.

PubMed: 35787552
DOI: 10.1107/S2053230X22005738

実験手法

X-RAY DIFFRACTION (2.27 Å)