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-Structure paper
タイトル | Structures of the mycobacterial MmpL4 and MmpL5 transporters provide insights into their role in siderophore export and iron acquisition. |
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ジャーナル・号・ページ | PLoS Biol, Vol. 22, Issue 10, Page e3002874, Year 2024 |
掲載日 | 2024年10月18日 |
![]() | Rakesh Maharjan / Zhemin Zhang / Philip A Klenotic / William D Gregor / Marios L Tringides / Meng Cui / Georgiana E Purdy / Edward W Yu / ![]() |
PubMed 要旨 | The Mycobacterium tuberculosis (Mtb) pathogen, the causative agent of the airborne infection tuberculosis (TB), harbors a number of mycobacterial membrane protein large (MmpL) transporters. These ...The Mycobacterium tuberculosis (Mtb) pathogen, the causative agent of the airborne infection tuberculosis (TB), harbors a number of mycobacterial membrane protein large (MmpL) transporters. These membrane proteins can be separated into 2 distinct subclasses, where they perform important functional roles, and thus, are considered potential drug targets to combat TB. Previously, we reported both X-ray and cryo-EM structures of the MmpL3 transporter, providing high-resolution structural information for this subclass of the MmpL proteins. Currently, there is no structural information available for the subclass associated with MmpL4 and MmpL5, transporters that play a critical role in iron homeostasis of the bacterium. Here, we report cryo-EM structures of the M. smegmatis MmpL4 and MmpL5 transporters to resolutions of 2.95 Å and 3.00 Å, respectively. These structures allow us to propose a plausible pathway for siderophore translocation via these 2 transporters, an essential step for iron acquisition that enables the survival and replication of the mycobacterium. |
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手法 | EM (単粒子) |
解像度 | 2.81 - 3.0 Å |
構造データ | EMDB-44167, PDB-9b43: EMDB-44171, PDB-9b46: EMDB-47097, PDB-9dp6: |
化合物 | ![]() ChemComp-PNS: |
由来 |
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![]() | TRANSPORT PROTEIN / Siderophore / MmpL4 / Mycolicibacterium smegmatis / MmpL5 / AcpM |