5TS9

Crystal structure of Chorismate mutase from Burkholderia phymatum

5TS9 の概要

• エントリーDOI: 10.2210/pdb5ts9/pdb
• 分子名称: Chorismate mutase (2 entities in total)
• 機能のキーワード: ssgcid, chorismate mutase, burkholderia phymatum, structural genomics, seattle structural genomics center for infectious disease, isomerase
• 由来する生物種: Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 150401.22

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2016-10-28, 公開日: 2016-11-23, 最終更新日: 2024-10-23)

主引用文献

Asojo, O.A.,Subramanian, S.,Abendroth, J.,Exley, I.,Lorimer, D.D.,Edwards, T.E.,Myler, P.J.
Crystal structure of chorismate mutase from Burkholderia phymatum.
Acta Crystallogr F Struct Biol Commun, 74:187-192, 2018

PubMed Abstract: The bacterium Burkholderia phymatum is a promiscuous symbiotic nitrogen-fixating bacterium that belongs to one of the largest groups of Betaproteobacteria. Other Burkholderia species are known to cause disease in plants and animals, and some are potential agents for biological warfare. Structural genomics efforts include characterizing the structures of enzymes from pathways that can be targeted for drug development. As part of these efforts, chorismate mutase from B. phymatum was produced and crystallized, and a 1.95 Å resolution structure is reported. This enzyme shares less than 33% sequence identity with other homologs of known structure. There are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQγ has reported roles in virulence. Chorismate mutase from B. phymatum has the prototypical AroQγ topology and retains the characteristic chorismate mutase active site. This suggests that substrate-based chorismate mutase inhibitors will not be specific and are likely to affect beneficial bacteria such as B. phymatum.

PubMed: 29633965
DOI: 10.1107/S2053230X18002868

実験手法

X-RAY DIFFRACTION (1.95 Å)