3JYY

SeMet LinB complexed with PPi

3JYY の概要

• エントリーDOI: 10.2210/pdb3jyy/pdb
• 関連するPDBエントリー: 3JZ0
• 分子名称: Lincosamide nucleotidyltransferase, MAGNESIUM ION, PYROPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha-beta structure, transferase
• 由来する生物種: Enterococcus faecium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68309.04

構造登録者

Morar, M.,Wright, G.D. (登録日: 2009-09-22, 公開日: 2009-11-03, 最終更新日: 2024-10-16)

主引用文献

Morar, M.,Bhullar, K.,Hughes, D.W.,Junop, M.,Wright, G.D.
Structure and mechanism of the lincosamide antibiotic adenylyltransferase LinB.
Structure, 17:1649-1659, 2009

PubMed Abstract: Lincosamides make up an important class of antibiotics used against a wide range of pathogens, including methicillin-resistant Staphylococcus aureus. Predictably, lincosamide-resistant microorganisms have emerged with antibiotic modification as one of their major resistance strategies. Inactivating enzymes LinB/A catalyze adenylylation of the drug; however, little is known about their mechanistic and structural properties. We determined two X-ray structures of LinB: ternary substrate- and binary product-bound complexes. Structural and kinetic characterization of LinB, mutagenesis, solvent isotope effect, and product inhibition studies are consistent with a mechanism involving direct in-line nucleotidyl transfer. The characterization of LinB enabled its classification as a member of a nucleotidyltransferase superfamily, along with nucleotide polymerases and aminoglycoside nucleotidyltransferases, and this relationship offers further support for the LinB mechanism. The LinB structure provides an evolutionary link to ancient nucleotide polymerases and suggests that, like protein kinases and acetyltransferases, these are proto-resistance elements from which drug resistance can evolve.

PubMed: 20004168
DOI: 10.1016/j.str.2009.10.013

実験手法

X-RAY DIFFRACTION (2.1 Å)