3uzu: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 11: Line 11:
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RSMA_BURP1 RSMA_BURP1]] Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity).  
[[http://www.uniprot.org/uniprot/RSMA_BURP1 RSMA_BURP1]] Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity).  
==See Also==
*[[Adenosine dimethyltransferase|Adenosine dimethyltransferase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 15:21, 12 October 2017

The structure of the Ribosomal RNA small subunit methyltransferase A from Burkholderia pseudomalleiThe structure of the Ribosomal RNA small subunit methyltransferase A from Burkholderia pseudomallei

Structural highlights

3uzu is a 1 chain structure with sequence from "bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:rsmA, ksgA, BURPS1710b_0874 ("Bacillus pseudomallei" Whitmore 1913)
Activity:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase, with EC number 2.1.1.182
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RSMA_BURP1] Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity).

3uzu, resolution 1.75Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA