5GOV

Crystal Structure of MCR-1, a phosphoethanolamine transferase, extracellular domain

5GOV の概要

• エントリーDOI: 10.2210/pdb5gov/pdb
• 分子名称: Probable phosphatidylethanolamine transferase Mcr-1, ZINC ION (3 entities in total)
• 機能のキーワード: mcr-1, petn transferase, zinc-binding, phosphorylation, colistin, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82124.45

構造登録者

Hu, M.,Guo, J.,Chen, S.,Hao, Q. (登録日: 2016-07-29, 公開日: 2016-12-21, 最終更新日: 2024-11-20)

主引用文献

Hu, M.,Guo, J.,Cheng, Q.,Yang, Z.,Chan, E.W.C.,Chen, S.,Hao, Q.
Crystal Structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for Colistin Resistance.
Sci Rep, 6:38793-38793, 2016

PubMed Abstract: MCR-1 is a phosphoethanolamine (pEtN) transferase that modifies the pEtN moiety of lipid A, conferring resistance to colistin, which is an antibiotic belonging to the class of polypeptide antibiotics known as polymyxins and is the last-line antibiotic used to treat multidrug resistant bacterial infections. Here we determined the crystal structure of the catalytic domain of MCR-1 (MCR-1-ED), which is originated in Escherichia coli (E. coli). MCR-1-ED was found to comprise several classical β-α-β-α motifs that constitute a "sandwich" conformation. Two interlaced molecules with different phosphorylation status of the residue T285 could give rise to two functional statuses of MCR-1 depending on the physiological conditions. MCR-1, like other known pEtN transferases, possesses an enzymatic site equipped with zinc binding residues. Interestingly, two zinc ions were found to mediate intermolecular interactions between MCR-1-ED molecules in one asymmetric unit and hence concatenation of MCR-1, allowing the protein to be oligomer. Findings of this work shall provide important insight into development of effective and clinically useful inhibitors of MCR-1 or structurally similar enzymes.

PubMed: 27958270
DOI: 10.1038/srep38793

実験手法

X-RAY DIFFRACTION (2.33 Å)