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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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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Structural genomics, unknown function
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Title:
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Crystal structure of the conserved hypothetical protein tt1887 from thermus thermophilus hb8
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Structure:
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Conserved hypothetical protein tt1887. Chain: a, b. Synonym: possible lysine decarboxylase. Engineered: yes
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Source:
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Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Tetramer (from
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Resolution:
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1.80Å
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R-factor:
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0.185
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R-free:
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0.223
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Authors:
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M.Kukimoto-Niino,K.Murayama,M.Idaka,T.Terada,M.Shirouzu,S.Kuramitsu, S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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M.Kukimoto-Niino
et al.
(2004).
Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8.
Protein Sci,
13,
3038-3042.
PubMed id:
DOI:
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Date:
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25-May-04
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Release date:
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25-Nov-04
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PROCHECK
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Headers
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References
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Q5SLJ9
(Q5SLJ9_THET8) -
DNA-binding protein from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq:
Struc:
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171 a.a.
171 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Protein Sci
13:3038-3042
(2004)
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PubMed id:
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Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8.
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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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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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Selected figure(s)
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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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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Ko,
R.Nishihama,
and
J.R.Pringle
(2008).
Control of 5-FOA and 5-FU resistance by Saccharomyces cerevisiae YJL055W.
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Yeast,
25,
155-160.
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W.B.Jeon,
S.T.Allard,
C.A.Bingman,
E.Bitto,
B.W.Han,
G.E.Wesenberg,
and
G.N.Phillips
(2006).
X-ray crystal structures of the conserved hypothetical proteins from Arabidopsis thaliana gene loci At5g11950 and AT2g37210.
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Proteins,
65,
1051-1054.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
