1MM4

Solution NMR structure of the outer membrane enzyme PagP in DPC micelles

Summary for 1MM4

• Entry DOI: 10.2210/pdb1mm4/pdb
• Related: 1MM5
• NMR Information: BMRB: 5557
• Descriptor: CrcA protein (1 entity in total)
• Functional Keywords: beta barrel, palmitoyltransferase, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 20198.43

Authors

Hwang, P.M.,Choy, W.-Y.,Lo, E.I.,Chen, L.,Forman-Kay, J.D.,Raetz, C.R.H.,Prive, G.G.,Bishop, R.E.,Kay, L.E. (deposition date: 2002-09-03, release date: 2002-09-13, Last modification date: 2024-05-22)

Primary citation

Hwang, P.M.,Choy, W.-Y.,Lo, E.I.,Chen, L.,Forman-Kay, J.D.,Raetz, C.R.H.,Prive, G.G.,Bishop, R.E.,Kay, L.E.
Solution Structure and Dynamics of the Outer Membrane Enzyme PagP by NMR
Proc.Natl.Acad.Sci.USA, 99:13560-13565, 2002

PubMed Abstract: The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response. The global fold of Escherichia coli PagP was determined in both dodecylphosphocholine and n-octyl-beta-d-glucoside detergent micelles using solution NMR spectroscopy. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha helix. The beta-barrel is well defined, whereas NMR relaxation measurements reveal considerable mobility in the loops connecting individual beta-strands. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface, positioning them optimally to interact with the polar headgroups of lipid A. Hence, the active site of PagP is situated on the outer surface of the outer membrane. Because the phospholipids that donate palmitate in the enzymatic reaction are normally found only in the inner leaflet of the outer membrane, PagP activity may depend on the aberrant migration of phospholipids into the outer leaflet. This finding is consistent with an emerging paradigm for outer membrane enzymes in providing an adaptive response toward disturbances in the outer membrane.

PubMed: 12357033
DOI: 10.1073/pnas.212344499

Experimental method

SOLUTION NMR