PDBsum entry: 1wy7

Transferase

PDB id: 1wy7

Contents

Protein chains

196 a.a. *

Ligands

SAH ×4

Waters ×312

* Residue conservation analysis

PDB id:

1wy7

Name:

Transferase

Title:

Crystal structure of a putative RNA methyltransferase ph1948 pyrococcus horikoshii

Structure:

Hypothetical protein ph1948. Chain: a, b, c, d. Engineered: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Gene: ph1948. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.242 R-free: 0.268

Authors:

Y.G.Gao,M.Yao,I.Tanaka

Key ref:

Y.G.Gao et al. (2005). Crystal structure of the putative RNA methyltransferase PH1948 from Pyrococcus horikoshii, in complex with the copurified S-adenosyl-L-homocysteine. Proteins, 61, 1141-1145. PubMed id: 16245322 DOI: 10.1002/prot.20678

Date:

08-Feb-05 Release date: 13-Dec-05

Protein chains

O59611  (O59611_PYRHO) -  Putative uncharacterized protein PH1948

Seq: 207 a.a.

Struc: 196 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: methylation (1 term)
• Biochemical function: nucleic acid binding (2 terms)

DOI no: 10.1002/prot.20678

Proteins 61:1141-1145 (2005)

PubMed id: 16245322

Crystal structure of the putative RNA methyltransferase PH1948 from Pyrococcus horikoshii, in complex with the copurified S-adenosyl-L-homocysteine.

Y.G.Gao, M.Yao, Z.Yong, I.Tanaka.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. PH1948 in complex with SAH and the omit map of SAH. (a) The protein is shown as a ribbon representation, and SAH as a stick model. The secondary structural elements are labeled 1- 7, A- E, and Z, consistent with standard nomenclature among MTases except for an additional helix, N, in the N-terminus. (b) A ball-and-stick model of SAH superimposed with the omit map. The map was calculated with coefficients F[o] - F[c] contoured at 2.5 calculated without SAH.

Figure 2.
Figure 2. Protein PH1948-SAH complex and structural comparison with ErmC . (a) Stick model showing the interaction of PH1948 and SAH. SAH is shown in green and the important protein residues in gray, labeled with the single-letter abbreviations. Oxygen atoms and water are shown in red, nitrogen atoms in blue, and sulfur atoms in brown. The interactions among protein, SAH, and water are indicated by dashed lines. (b) Structural comparison of PH1948 with the N-terminal catalytic domain of ErmC . The two structures are shown as ribbons, with the similar fold in gray, and varying parts in red (PH1948) and blue (ErmC ). The residues in the catalytic site are shown as sticks, and the cofactor SAH as lines. The sequences of the peptide segments possibly involved in substrate binding are compared: identity (*), strong similarity (:), and weak similarity (.), respectively.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 1141-1145) copyright 2005.