1pys: Difference between revisions

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[[Image:1pys.~~jpg~~|left|200px]]

[[Image:1pys.png|left|200px]]

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~~'''~~PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS~~'''~~

===PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS===

~~==Overview==~~

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The ~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_7664121}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7664121 is the PubMed ID number.

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==About this Structure==

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[[Category: Sh3 domain]]

[[Category: Thermus thermophilus]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 05~~:39:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:16:20 2008''

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-[[Image:1pys.jpg|left|200px]]
+{{Seed}}
+[[Image:1pys.png|left|200px]]
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 {{STRUCTURE_1pys|  PDB=1pys  |  SCENE=  }}
-'''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''
+===PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS===
-==Overview==
+<!--
-The 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664121}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664121 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7664121}}
 ==About this Structure==
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 [[Category: Sh3 domain]]
 [[Category: Thermus thermophilus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:39:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:16:20 2008''