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PDBsum entry 1k9x
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Carboxypeptidase
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PDB id
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1k9x
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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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Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon pyrococcus furiosus.
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Authors
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J.W.Arndt,
B.Hao,
V.Ramakrishnan,
T.Cheng,
S.I.Chan,
M.K.Chan.
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Ref.
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Structure, 2002,
10,
215-224.
[DOI no: ]
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PubMed id
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Abstract
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The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been
determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD)
methods. PfuCP represents the first structure of the new M32 family of
carboxypeptidases. The overall structure is comprised of a homodimer. Each
subunit is mostly helical with its most pronounced feature being a deep
substrate binding groove. The active site lies at the bottom of this groove and
contains an HEXXH motif that coordinates the metal ion required for catalysis.
Surprisingly, the structure is similar to the recently reported rat neurolysin.
Comparison of these structures as well as sequence analyses with other
homologous proteins reveal several conserved residues. The roles for these
conserved residues in the catalytic mechanism are inferred based on modeling and
their location.
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Figure 3.
Figure 3. PfuCP Subunit Structure(A) Ribbons diagram of a
single PfuCP subunit as viewed along the substrate groove. Drawn
in stereo (active site metal, pink).(B) Surface diagram of PfuCP
subunit in stereo (negatively charged residues, red; positively
charged residues, blue) modeled with 10-mer polyalanine
substrate.(C) Rainbow stereo plot of the C[a] trace of PfuCP
subunit (N terminus, blue; C terminus, red; active site metal,
pink). Every twentieth residue is labeled. Figures were prepared
using the programs MOLSCRIPT, Raster-3D, and GRASP [11, 29 and
35].
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
215-224)
copyright 2002.
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