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PDBsum entry 1n51
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Hydrolase/hydrolase inhibitor
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PDB id
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1n51
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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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Structure of escherichia coli aminopeptidase p in complex with the inhibitor apstatin.
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Authors
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S.C.Graham,
M.J.Maher,
W.H.Simmons,
H.C.Freeman,
J.M.Guss.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
1770-1779.
[DOI no: ]
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PubMed id
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Abstract
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Aminopeptidase P (APPro) is a metalloprotease whose active site includes a
dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from
a polypeptide when the second residue is proline. A complex of Escherichia coli
APPro (EcAPPro) with an inhibitor, apstatin
[N-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl-L-prolyl-L-prolyl-L-alaninamide],
has been crystallized. Apstatin binds to the active site of EcAPPro with its
N-terminal amino group coordinated to one of the two Mn(II) atoms at the metal
centre. The apstatin hydroxyl group replaces a hydroxide ion which bridges the
two metal atoms in the native enzyme. The first proline residue of apstatin lies
in a small hydrophobic cleft. The structure of the apstatin-EcAPPro complex has
been refined at 2.3 A resolution with residuals R = 0.179 and R(free) = 0.204.
The structure of the complex illustrates how apstatin inhibits APPro and
suggests how substrates may bind to the enzyme, but the basis of the
proline-specificity remains elusive.
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Figure 4.
Figure 4
Stereoview of apstatin bound at the active site. The magenta spheres represent the MnII
atoms. Only protein residues coordinating the metal atoms or forming hydrogen bonds with
apstatin are shown. The `omit' F[o] - F[c] electron-density difference map calculated
before apstatin was included in the model is contoured at 3 [168][sigma] .
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Figure 6.
Figure 6
Two-dimensional schematic diagram showing the interactions between apstatin and EcAPPro.
Hydrogen bonds (green dashed lines), inhibitor-metal ligand interactions (purple sticks)
and hydrophobic interactions (red combs) a
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
1770-1779)
copyright 2004.
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Secondary reference #1
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Title
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Crystallography & nmr system: a new software suite for macromolecular structure determination.
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Authors
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A.T.Brünger,
P.D.Adams,
G.M.Clore,
W.L.Delano,
P.Gros,
R.W.Grosse-Kunstleve,
J.S.Jiang,
J.Kuszewski,
M.Nilges,
N.S.Pannu,
R.J.Read,
L.M.Rice,
T.Simonson,
G.L.Warren.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
905-921.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1.
CNS
consists of five layers which are under user control. The
high-level HTML graphical interface interacts with the task-
oriented input files. The task files make use of the
CNS
language
and the modules. The modules contain
CNS
language statements.
The CNS
language is interpreted by the
CNS
FORTRAN77
program. The program performs the data manipulations, data
operations, and 'hard-wired' algorithms.
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Figure 3.
Fig. 3. (a) Example of a
CNS
HTML
form page. This particular
example corresponds to the task
file in Fig. 6.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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