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TitleThe substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 7969-7981, Year 2018
Publish dateJul 28, 2017 (structure data deposition date)
AuthorsBohl, T.E. / Ieong, P. / Lee, J.K. / Lee, T. / Kankanala, J. / Shi, K. / Demir, O. / Kurahashi, K. / Amaro, R.E. / Wang, Z. / Aihara, H.
External linksJ. Biol. Chem. / PubMed:29626094
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-5wly:
E. coli LpxH- 8 mutations
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-FMT:
FORMIC ACID

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / lipid A synthesis / open conformation / UDP-diacyl-glucosamine pyrophosphohydrolase / apha/beta-hydrolase

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