1zl3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zl3.gif|left|200px]]<br /><applet load="1zl3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1zl3.gif|left|200px]]
-
caption="1zl3, resolution 2.80&Aring;" />
+
 
-
'''Coupling of active site motions and RNA binding'''<br />
+
{{Structure
 +
|PDB= 1zl3 |SIZE=350|CAPTION= <scene name='initialview01'>1zl3</scene>, resolution 2.80&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70]
 +
|GENE= truB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
}}
 +
 
 +
'''Coupling of active site motions and RNA binding'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1ZL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZL3 OCA].
+
1ZL3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZL3 OCA].
==Reference==
==Reference==
-
Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain., Hoang C, Hamilton CS, Mueller EG, Ferre-D'Amare AR, Protein Sci. 2005 Aug;14(8):2201-6. Epub 2005 Jun 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15987897 15987897]
+
Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain., Hoang C, Hamilton CS, Mueller EG, Ferre-D'Amare AR, Protein Sci. 2005 Aug;14(8):2201-6. Epub 2005 Jun 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15987897 15987897]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
Line 23: Line 32:
[[Category: rna-modification]]
[[Category: rna-modification]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:41 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:36:50 2008''

Revision as of 13:36, 20 March 2008


PDB ID 1zl3

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Gene: truB (Escherichia coli)
Activity: Pseudouridylate synthase, with EC number 4.2.1.70
Coordinates: save as pdb, mmCIF, xml



Coupling of active site motions and RNA binding


Overview

The pseudouridine synthase TruB is responsible for the universally conserved post-transcriptional modification of residue 55 of elongator tRNAs. In addition to the active site, the "thumb", a peripheral domain unique to the TruB family of enzymes, makes extensive interactions with the substrate. To coordinate RNA binding and release with catalysis, the thumb may be able to sense progress of the reaction in the active site. To establish whether there is a structural correlate of communication between the active site and the RNA-sequestering thumb, we have solved the structure of a catalytically inactive point mutant of TruB in complex with a substrate RNA, and compared it to the previously determined structure of an active TruB bound to a reaction product. Superposition of the two structures shows that they are extremely similar, except in the active site and, intriguingly, in the relative position of the thumb. Because the two structures were solved using isomorphous crystals, and because the thumb is very well ordered in both structures, the displacement of the thumb we observe likely reflects preferential propagation of active site perturbations to this RNA-binding domain. One of the interactions between the active site and the thumb involves an active site residue whose hydrogen-bonding status changes during the reaction. This may allow the peripheral RNA-binding domain to monitor progress of the pseudouridylation reaction.

About this Structure

1ZL3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain., Hoang C, Hamilton CS, Mueller EG, Ferre-D'Amare AR, Protein Sci. 2005 Aug;14(8):2201-6. Epub 2005 Jun 29. PMID:15987897

Page seeded by OCA on Thu Mar 20 15:36:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools