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PDBsum entry 1mdx
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural studies of salmonella typhimurium arnb (pmrh) aminotransferase: a 4-Amino-4-Deoxy-L-Arabinose lipopolysaccharide-Modifying enzyme.
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Authors
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B.W.Noland,
J.M.Newman,
J.Hendle,
J.Badger,
J.A.Christopher,
J.Tresser,
M.D.Buchanan,
T.A.Wright,
M.E.Rutter,
W.E.Sanderson,
H.J.Müller-Dieckmann,
K.S.Gajiwala,
S.G.Buchanan.
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Ref.
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Structure, 2002,
10,
1569-1580.
[DOI no: ]
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PubMed id
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Abstract
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Lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain
pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial
peptides, including those derived from the innate immune system. ArnB catalysis
of amino group transfer from glutamic acid to the 4"-position of a
UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose
represents a key step in the lipid A modification pathway. Structural and
functional studies of the ArnB aminotransferase were undertaken by combining
X-ray crystallography with biochemical analyses. High-resolution crystal
structures were solved for two native forms and one covalently inhibited form of
S. typhimurium ArnB. These structures permitted identification of key residues
involved in substrate binding and catalysis, including a rarely observed
nonprolyl cis peptide bond in the active site.
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Figure 7.
Figure 7. Proposed ArnB Enzyme Mechanism(A) The first
half-reaction.(B) The second half-reaction. The lysine residue
is Lys188.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1569-1580)
copyright 2002.
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Secondary reference #1
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Title
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Structural analysis of a set of proteins resulting from a bacterial genomics project.
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Authors
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J.Badger,
J.M.Sauder,
J.M.Adams,
S.Antonysamy,
K.Bain,
M.G.Bergseid,
S.G.Buchanan,
M.D.Buchanan,
Y.Batiyenko,
J.A.Christopher,
S.Emtage,
A.Eroshkina,
I.Feil,
E.B.Furlong,
K.S.Gajiwala,
X.Gao,
D.He,
J.Hendle,
A.Huber,
K.Hoda,
P.Kearins,
C.Kissinger,
B.Laubert,
H.A.Lewis,
J.Lin,
K.Loomis,
D.Lorimer,
G.Louie,
M.Maletic,
C.D.Marsh,
I.Miller,
J.Molinari,
H.J.Muller-Dieckmann,
J.M.Newman,
B.W.Noland,
B.Pagarigan,
F.Park,
T.S.Peat,
K.W.Post,
S.Radojicic,
A.Ramos,
R.Romero,
M.E.Rutter,
W.E.Sanderson,
K.D.Schwinn,
J.Tresser,
J.Winhoven,
T.A.Wright,
L.Wu,
J.Xu,
T.J.Harris.
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Ref.
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Proteins, 2005,
60,
787-796.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. Ribbon diagrams[54] of the eleven structures
described in the Results and Discussion section: (A) monomer
from the dapE structure (1VGY), (B) homodimer from the nudE
structure (1VHG), (C) monomer from the DUS structure (1VHN), (D)
monomer from the ysdC structure, 1VHE, (E) monomer from the frwX
structure, 1VHO, (F) monomer from the perB structure (1VIZ), (G)
monomer from the plsX structure (1VI1), (H) monomer from the
yqgF structure (1VHX), (I) monomer from the yigZ structure
(1VI7), (J) monomer from the YiiM structure (1O65), (K) the
novel sufD structure (1VH4) with the homodimer interface in the
center.
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The above figure is
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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