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PDBsum entry 2as0
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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 ph1915 (apc 5817): a hypothetical RNA methyltransferase
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Structure:
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Hypothetical protein ph1915. Chain: a, b. Engineered: yes
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Source:
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Pyrococcus horikoshii. Organism_taxid: 53953. Gene: ph1915. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Biol. unit:
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Dimer (from
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Resolution:
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1.80Å
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R-factor:
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0.207
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R-free:
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0.239
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Authors:
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W.Sun,X.Xu,M.Pavlova,A.M.Edwards,A.Joachimiak,A.Savchenko, D.Christendat,Midwest Center For Structural Genomics (Mcsg)
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Key ref:
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W.Sun
et al.
(2005).
The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii.
Protein Sci,
14,
3121-3128.
PubMed id:
DOI:
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Date:
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22-Aug-05
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Release date:
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20-Sep-05
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PROCHECK
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Headers
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References
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O59578
(O59578_PYRHO) -
PUA domain-containing protein from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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Seq:
Struc:
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396 a.a.
396 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
14:3121-3128
(2005)
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PubMed id:
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The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii.
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W.Sun,
X.Xu,
M.Pavlova,
A.M.Edwards,
A.Joachimiak,
A.Savchenko,
D.Christendat.
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ABSTRACT
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The S-adenosyl-L-methionine (SAM)-dependent methyltransferases represent a
diverse and biologically important class of enzymes. These enzymes utilize the
ubiquitous methyl donor SAM as a cofactor to methylate proteins, small
molecules, lipids, and nucleic acids. Here we present the crystal structure of
PH1915 from Pyrococcus horikoshii OT3, a predicted SAM-dependent
methyltransferase. This protein belongs to the Cluster of Orthologous Group
1092, and the presented crystal structure is the first representative structure
of this protein family. Based on sequence and 3D structure analysis, we have
made valuable functional insights that will facilitate further studies for
characterizing this group of proteins. Specifically, we propose that PH1915 and
its orthologs are rRNA- or tRNA-specific methyltransferases.
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Selected figure(s)
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Figure 2.
Figure 2. Ribbon diagrams of the individual domains of
PH1915. (A) Domain N1.  -Helices are
colored red, and  -strands are
colored blue. The overall topology of the N1 domain is analogous
to the PUA domain. (B) Domain N2. -Helices are
colored green, whereas -strands are
colored orange. (C) C-terminal domain. -helices are
colored light blue, and -strands are
colored yellow. This C-terminal domain is reminiscent of the SAM
cofactor binding domain seen in other MTases.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2005,
14,
3121-3128)
copyright 2005.
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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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M.Umitsu,
H.Nishimasu,
A.Noma,
T.Suzuki,
R.Ishitani,
and
O.Nureki
(2009).
Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2.
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Proc Natl Acad Sci U S A,
106,
15616-15621.
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PDB codes:
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I.Pérez-Arellano,
J.Gallego,
and
J.Cervera
(2007).
The PUA domain - a structural and functional overview.
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FEBS J,
274,
4972-4984.
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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
