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| | {{STRUCTURE_1zl3| PDB=1zl3 | SCENE= }} | | {{STRUCTURE_1zl3| PDB=1zl3 | SCENE= }} |
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| - | '''Coupling of active site motions and RNA binding'''
| + | ===Coupling of active site motions and RNA binding=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15987897}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15987897 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15987897}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Product release]] | | [[Category: Product release]] |
| | [[Category: Rna-modification]] | | [[Category: Rna-modification]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:45:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:46:40 2008'' |
Revision as of 07:46, 28 July 2008
Template:STRUCTURE 1zl3
Coupling of active site motions and RNA binding
Template:ABSTRACT PUBMED 15987897
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 Mon Jul 28 10:46:40 2008
