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PDBsum entry 3oii
Go to PDB code:
Ribosomal protein
PDB id
3oii
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Contents
Protein chains
216 a.a.
*
Ligands
SAH
×2
GOL
Waters
×224
*
Residue conservation analysis
PDB id:
3oii
Links
PDBe
RCSB
MMDB
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Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Sacch3D
Name:
Ribosomal protein
Title:
Crystal structure of saccharomyces cerevisiae nep1/emg1 bound to s- adenosylhomocysteine
Structure:
Essential for mitotic growth 1. Chain: a, b. Synonym: nucleolar essential protein 1. Engineered: yes
Source:
Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: emg1, nep1, ylr186w, l9470.5. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.85Å
R-factor:
0.174
R-free:
0.216
Authors:
S.R.Thomas,A.Szyk,N.Laronde-Leblanc
Key ref:
S.R.Thomas et al. (2011). Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis.
Nucleic Acids Res
,
39
, 2445-2457.
PubMed id:
21087996
Date:
19-Aug-10
Release date:
01-Dec-10
PROCHECK
Headers
References
Protein chains
Q06287
(NEP1_YEAST) - Ribosomal RNA small subunit methyltransferase NEP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
252 a.a.
216 a.a.
Key:
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.2.1.1.260
- rRNA small subunit pseudouridine methyltransferase Nep1.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
pseudouridine
1191
in yeast 18S rRNA + S-adenosyl-L-methionine = N
1
- methylpseudouridine
1191
in yeast 18S rRNA + S-adenosyl-L-homocysteine + H
+
pseudouridine(1191) in yeast 18S rRNA
+
S-adenosyl-L-methionine
=
N(1)- methylpseudouridine(1191) in yeast 18S rRNA
+
S-adenosyl-L-homocysteine
+
H(+)
Bound ligand (Het Group name =
SAH
)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Added reference
Nucleic Acids Res
39
:2445-2457 (2011)
PubMed id:
21087996
Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis.
S.R.Thomas,
C.A.Keller,
A.Szyk,
J.R.Cannon,
N.A.Laronde-Leblanc.
ABSTRACT
No abstract given.
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