1pys: Difference between revisions
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==PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS== | ==PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS== | ||
<StructureSection load='1pys' size='340' side='right' caption='[[1pys]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1pys' size='340' side='right'caption='[[1pys]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pys]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PYS FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pys]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PYS FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1pys" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1pys" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Phenylalanine--tRNA ligase]] | [[Category: Phenylalanine--tRNA ligase]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
Revision as of 13:10, 27 November 2019
PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUSPHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.,Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG Nat Struct Biol. 1995 Jul;2(7):537-47. PMID:7664121[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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