2bh2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2bh2 |SIZE=350|CAPTION= <scene name='initialview01'>2bh2</scene>, resolution 2.15Å | |PDB= 2bh2 |SIZE=350|CAPTION= <scene name='initialview01'>2bh2</scene>, resolution 2.15Å | ||
|SITE= <scene name='pdbsite=AC1:Fmu+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fmu+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=FMU:5-FLUORO-5-METHYLURIDINE-5'-MONOPHOSPHATE'>FMU</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh2 OCA], [http://www.ebi.ac.uk/pdbsum/2bh2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bh2 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Lee, T T.]] | [[Category: Lee, T T.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: SAH]] | ||
| - | [[Category: SF4]] | ||
[[Category: 4fe-4]] | [[Category: 4fe-4]] | ||
[[Category: base flipping]] | [[Category: base flipping]] | ||
| Line 45: | Line 46: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:19 2008'' |
Revision as of 23:06, 30 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF E. COLI 5-METHYLURIDINE METHYLTRANSFERASE RUMA IN COMPLEX WITH RIBOSOMAL RNA SUBSTRATE AND S-ADENOSYLHOMOCYSTEINE.
Overview
A single base (U1939) within E. coli 23S ribosomal RNA is methylated by its dedicated enzyme, RumA. The structure of RumA/RNA/S-adenosylhomocysteine uncovers the mechanism for achieving unique selectivity. The single-stranded substrate is "refolded" on the enzyme into a compact conformation with six key intra-RNA interactions. The RNA substrate contributes directly to catalysis. In addition to the target base, a second base is "flipped out" from the core loop to stack against the adenine of the cofactor S-adenosylhomocysteine. Nucleotides in permuted sequence order are stacked into the site vacated by the everted target U1939 and compensate for the energetic penalty of base eversion. The 3' hairpin segment of the RNA binds distal to the active site and provides binding energy that contributes to enhanced catalytic efficiency. Active collaboration of RNA in catalysis leads us to conclude that RumA and its substrate RNA may reflect features from the earliest RNA-protein era.
About this Structure
2BH2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function., Lee TT, Agarwalla S, Stroud RM, Cell. 2005 Mar 11;120(5):599-611. PMID:15766524
Page seeded by OCA on Mon Mar 31 02:06:19 2008
Categories: Escherichia coli | Single protein | Agarwalla, S. | Lee, T T. | Stroud, R M. | 4fe-4 | Base flipping | Base stacking | Direct protein sequencing | General base | Iron-sulfur cluster | Metal-binding | Methyltransferase | Ob-fold | Product release | Protein-rna complex | Rna modification | Rna processing | Ruma | Sam | Substrate selectivity | Transferase
