1jbm: Difference between revisions

New page: left|200px<br /><applet load="1jbm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jbm, resolution 1.85Å" /> '''Heptameric crystal s...
 
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[[Image:1jbm.jpg|left|200px]]<br /><applet load="1jbm" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jbm.jpg|left|200px]]<br /><applet load="1jbm" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jbm, resolution 1.85&Aring;" />
caption="1jbm, resolution 1.85&Aring;" />
'''Heptameric crystal structure of Mth649, an Sm-like archaeal protein from Methanobacterium thermautotrophicum'''<br />
'''Heptameric crystal structure of Mth649, an Sm-like archaeal protein from Methanobacterium thermautotrophicum'''<br />


==Overview==
==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.
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==
==About this Structure==
1JBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with EDO and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JBM OCA].  
1JBM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBM OCA].  


==Reference==
==Reference==
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[[Category: ring-shaped homoheptamer]]
[[Category: ring-shaped homoheptamer]]


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