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PDBsum entry 4j6e
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PDB id:
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Hydrolase
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Title:
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Structure of lpxi d225a mutant
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Structure:
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Udp-2,3-diacylglucosamine pyrophosphatase lpxi. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Caulobacter crescentus. Organism_taxid: 565050. Strain: cb15n. Gene: 77330127, ccna_01987, cc_1910, lpxi. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.52Å
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R-factor:
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0.227
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R-free:
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0.286
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Authors:
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L.E.Metzger Iv,J.K.Lee,J.S.Finer-Moore,C.R.H.Raetz,R.M.Stroud,Center For Structures Of Membrane Proteins (Csmp)
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Key ref:
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L.E.Metzger
et al.
(2012).
LpxI structures reveal how a lipid A precursor is synthesized.
Nat Struct Biol,
19,
1132-1138.
PubMed id:
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Date:
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11-Feb-13
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Release date:
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08-May-13
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Supersedes:
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PROCHECK
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Headers
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References
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A0A0H3C8Q1
(A0A0H3C8Q1_CAUVN) -
UDP-2,3-diacylglucosamine pyrophosphatase LpxI from Caulobacter vibrioides (strain NA1000 / CB15N)
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Seq:
Struc:
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280 a.a.
273 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.6.1.54
- UDP-2,3-diacylglucosamine diphosphatase.
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Reaction:
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a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H2O = a lipid X + UMP + 2 H+
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UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
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+
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H2O
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=
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lipid X
Bound ligand (Het Group name = )
matches with 70.59% similarity
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+
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UMP
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+
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2
×
H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Nat Struct Biol
19:1132-1138
(2012)
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PubMed id:
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LpxI structures reveal how a lipid A precursor is synthesized.
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L.E.Metzger,
J.K.Lee,
J.S.Finer-Moore,
C.R.Raetz,
R.M.Stroud.
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ABSTRACT
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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.
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