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PDBsum entry 1weh
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Structural genomics, unknown function
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PDB id
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1weh
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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 structures of possible lysine decarboxylases from thermus thermophilus hb8.
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Authors
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M.Kukimoto-Niino,
K.Murayama,
M.Kato-Murayama,
M.Idaka,
Y.Bessho,
A.Tatsuguchi,
R.Ushikoshi-Nakayama,
T.Terada,
S.Kuramitsu,
M.Shirouzu,
S.Yokoyama.
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Ref.
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Protein Sci, 2004,
13,
3038-3042.
[DOI no: ]
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PubMed id
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Abstract
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TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical
proteins, and are annotated as possible lysine decarboxylases in the Pfam
database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 A
and 2.2 A resolutions, respectively, as determined by the multiwavelength
anomalous dispersion (MAD) method. TT1887 is a homotetramer, while TT1465 is a
homohexamer in the crystal and in solution. The structures of the TT1887 and
TT1465 monomers contain single domains with the Rossmann fold, comprising six
alpha helices and seven beta strands, and are quite similar to each other. The
major structural differences exist in the N terminus of TT1465, where there are
two additional alpha helices. A comparison of the structures revealed the
elements that are responsible for the different oligomerization modes. The
distributions of the electrostatic potential on the solvent-accessible surfaces
suggested putative active sites.
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Figure 2.
Figure 2. Ribbon representations of the TT1887 tetramer (A)
and the TT1465 hexamer (B) (stereo view). Each monomer is
colored differently. Electrostatic surface representations of
the TT1887 monomer (C) and the TT1465 monomer (D). Blue and red
surfaces represent positive and negative potentials,
respectively. The locations of putative active sites are shown
with arrows.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
3038-3042)
copyright 2004.
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