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PDBsum entry 2cb0
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References listed in PDB file
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Key reference
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Title
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The crystal structure of a novel glucosamine-6-Phosphate deaminase from the hyperthermophilic archaeon pyrococcus furiosus.
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Authors
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K.J.Kim,
M.H.Kim,
G.H.Kim,
B.S.Kang.
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Ref.
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Proteins, 2007,
68,
413-417.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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No abstract given.
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Figure 1.
Figure 1. Structures of glucosamine 6-phosphate deaminase from
P. furiosus. (A) A polypeptide chain consisted of two similar
five-stranded subdomains and C-terminal tail. N-terminal
subdomain (red and yellow) and C-terminal subdomain (blue and
magenta) were linked by short loop (gray) were followed by long
C-terminal coil region (gray). (B) Twofold symmetrical
interaction of two polypeptide chains (green and blue). A helix
(yellow) from one chain interacts a cleft between N- and
C-terminal subdomains of another chain (B_Nt and B_Ct) forming
an active site (red circle). (C) A substrate, glucosamine
6-phosphate (yellow) from crystal structure of the isomerase of
E. coli GlmS was superimposed on the active site of GlmD
consisted of both monomers (green and blue). (D) C-terminal tail
covers the substrate-binding site between two monomers (blue and
green). Glucosamine 6-phosphate is placed to the binding pocket.
Residue from other than a molecule containing sugar-binding site
are indicated by asterisk. Residues D320, R324, and W325 from
C-terminal region interact to K230, R226, and W249 from another
monomer.
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Figure 2.
Figure 2. The multiple sequence alignment of glucosamine
6-phsophate deaminases (GlmD) with glucosamine 6-phosphate
synthases (GlmS). Amino acid sequences of the GlmD (1-325) from
P. furiosus (Pfu_glmD), GlmD (1-326) and iosmerase domain
(252-602) of GlmS from T. kodakaraensis (Tko_Glms and Tko_GlmD),
and isomerase domain (249-608) of GlmS from E. coli (Eco_GlmS)
were aligned. Numbering shown is from P. furiosus GlmD. Shown
above alignments are elements of secondary structure of GlmD
from P. furiosus. Residues involved in glucosamine 6-phsophate
binding are marked with closed blue triangles. Multiple
alignment was done using the T-coffe software and visualized
using ESPript softwate both located on the ExPASy Proteomics
Server (http://au.expasy.org/).
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
68,
413-417)
copyright 2007.
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