1jbm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1jbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jbm, resolution 1.85&Aring;" /> '''Heptameric crystal s...)
Next diff →

Revision as of 15:57, 20 November 2007


1jbm, resolution 1.85Å

Drag the structure with the mouse to rotate

Heptameric crystal structure of Mth649, an Sm-like archaeal protein from Methanobacterium thermautotrophicum

Overview

Intron splicing is a prime example of the many types of RNA processing, catalyzed by small nuclear ribonucleoprotein (snRNP) complexes. Sm, proteins form the cores of most snRNPs, and thus to learn principles of, snRNP assembly we characterized the oligomerization and ligand-binding, properties of Sm-like archaeal proteins (SmAPs) from Pyrobaculum, aerophilum (Pae) and Methanobacterium thermautotrophicum (Mth)., Ultracentrifugation shows that Mth SmAP1 is exclusively heptameric in, solution, whereas Pae SmAP1 forms either disulfide-bonded 14-mers or, sub-heptameric states (depending on the redox potential). By electron, microscopy, we show that Pae and Mth SmAP1 polymerize into bundles of well, ordered fibers that probably form by head-to-tail stacking of heptamers., The crystallographic results reported here corroborate these findings by, showing heptamers and 14-mers of both Mth and Pae SmAP1 in four new, crystal forms. The 1.9 A-resolution structure of Mth SmAP1 bound to, uridine-5'-monophosphate (UMP) reveals conserved ligand-binding sites. The, likely RNA binding site in Mth agrees with that determined for, Archaeoglobus fulgidus (Afu) SmAP1. Finally, we found that both Pae and, Mth SmAP1 gel-shift negatively supercoiled DNA. These results distinguish, SmAPs from eukaryotic Sm proteins and suggest that SmAPs have a generic, single-stranded nucleic acid-binding activity.

About this Structure

1JBM is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with EDO and ACY as ligands. Full crystallographic information is available from OCA.

Reference

The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)., Mura C, Kozhukhovsky A, Gingery M, Phillips M, Eisenberg D, Protein Sci. 2003 Apr;12(4):832-47. PMID:12649441

Page seeded by OCA on Tue Nov 20 18:05:04 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools