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PDBsum entry 2zig
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of ttha0409, putative DNA modification methylase from thermus thermophilus hb8
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Structure:
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Putative modification methylase. Chain: a, b. Synonym: ttha0409. Engineered: yes
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Source:
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Thermus thermophilus. Organism_taxid: 274. Strain: hb8. Gene: ttha0409. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.10Å
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R-factor:
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0.233
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R-free:
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0.274
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Authors:
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R.Morita,H.Ishikawa,N.Nakagawa,R.Masui,S.Yokoyama,S.Kuramitsu,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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R.Morita
et al.
(2008).
Crystal structure of a putative DNA methylase TTHA0409 from Thermus thermophilus HB8.
Proteins,
73,
259-264.
PubMed id:
DOI:
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Date:
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15-Feb-08
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Release date:
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29-Jul-08
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PROCHECK
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Headers
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References
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Enzyme class 1:
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Chains A, B:
E.C.2.1.1.-
- ?????
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Enzyme class 2:
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Chains A, B:
E.C.2.1.1.113
- site-specific DNA-methyltransferase (cytosine-N(4)-specific).
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Reaction:
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a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N4-methyl- 2'-deoxycytidine in DNA + S-adenosyl-L-homocysteine + H+
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2'-deoxycytidine in DNA
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+
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S-adenosyl-L-methionine
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=
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N(4)-methyl- 2'-deoxycytidine in DNA
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+
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S-adenosyl-L-homocysteine
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proteins
73:259-264
(2008)
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PubMed id:
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Crystal structure of a putative DNA methylase TTHA0409 from Thermus thermophilus HB8.
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R.Morita,
H.Ishikawa,
N.Nakagawa,
S.Kuramitsu,
R.Masui.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. Crystal structure of TTHA0409. A: A ribbon model of
the overall structure of the ligand-free TTHA0409 dimer (PDB ID;
2ZIG). Rainbow coloring from blue through green to red indicates
the N- to C-terminal position of the residue in the model. B: A
ribbon model of the monomer structure of TTHA0409. -helices
(A-F), -strands
(1-10), and TRD are labeled. C: An electrostatic potential map
of the ligand-free TTHA0409 dimer. Positively and negatively
charged regions are indicated in blue and red, respectively. D:
Electrostatic potential map of the active site in the
AdoMet-bound TTHA0409 (PDB ID; 2ZIF). E: A ribbon model of the
structure of M.RsrI (PDB ID; 1NW5).
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Figure 2.
Figure 2. Dimer interface of TTHA0409 (A) and M.MboIIA (B).
Each picture on the left shows an enlarged image of the
interface including the 4-
5
region in the right picture. In (A), residues 97-115 in one
subunit (green) and residues 127-134 in the other subunit (blue)
are represented by sticks. Several residues in this region form
hydrogen bonds. In (B), residues 74 and 75 in one subunit
(green) and residues 89-92 in the other subunit (blue) are
represented by sticks. No residue in this region forms a
hydrogen bond.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
259-264)
copyright 2008.
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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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U.K.Madhusoodanan,
and
D.N.Rao
(2010).
Diversity of DNA methyltransferases that recognize asymmetric target sequences.
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Crit Rev Biochem Mol Biol,
45,
125-145.
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E.G.Malygin,
A.A.Evdokimov,
and
S.Hattman
(2009).
Dimeric/oligomeric DNA methyltransferases: an unfinished story.
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Biol Chem,
390,
835-844.
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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.
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