4GGM

Structure of LpxI

Summary for 4GGM

• Entry DOI: 10.2210/pdb4ggm/pdb
• Related: 4GGI
• Descriptor: UDP-2,3-diacylglucosamine pyrophosphatase LpxI, MAGNESIUM ION, (R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)TETRAHYDRO-2H-PYRAN-4-YL) 3-HYDROXYTETRADECANOATE, ... (4 entities in total)
• Functional Keywords: structural genomics, psi-biology, protein structure initiative, center for structures of membrane proteins, csmp, lipid binding, hydrolase
• Biological source: Caulobacter crescentus
• Total number of polymer chains: 1
• Total formula weight: 31113.07

Authors

Metzger IV, L.E.,Lee, J.K.,Finer-Moore, J.S.,Raetz, C.R.H.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2012-08-06, release date: 2012-10-03, Last modification date: 2024-11-06)

Primary citation

Metzger, L.E.,Lee, J.K.,Finer-Moore, J.S.,Raetz, C.R.,Stroud, R.M.
LpxI structures reveal how a lipid A precursor is synthesized.
Nat.Struct.Mol.Biol., 19:1132-1138, 2012

PubMed Abstract: Enzymes in lipid metabolism acquire and deliver hydrophobic substrates and products from within lipid bilayers. The structure at 2.55 Å of one isozyme of a constitutive enzyme in lipid A biosynthesis, LpxI from Caulobacter crescentus, has a novel fold. Two domains close around a completely sequestered substrate, UDP-2,3-diacylglucosamine, and open to release products either to the neighboring enzyme in a putative multienzyme complex or to the bilayer. Mutation analysis identifies Asp225 as key to Mg(2+)-catalyzed diphosphate hydrolysis. These structures provide snapshots of the enzymatic synthesis of a critical lipid A precursor.

PubMed: 23042606
DOI: 10.1038/nsmb.2393

Experimental method

X-RAY DIFFRACTION (2.897 Å)