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New page: left|200px<br /><applet load="1xty" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xty, resolution 1.8Å" /> '''Crystal structure of ...
 
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[[Image:1xty.gif|left|200px]]<br /><applet load="1xty" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xty.gif|left|200px]]<br /><applet load="1xty" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xty, resolution 1.8&Aring;" />
caption="1xty, resolution 1.8&Aring;" />
'''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase'''<br />
'''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase'''<br />


==Overview==
==Overview==
The 3-D structure of the peptidyl-tRNA hydrolase from the archaea, Sulfolobus solfataricus has been solved at 1.8 A resolution. Homologues of, this enzyme are found in archaea and eucarya. Bacteria display a different, type of peptidyl-tRNA hydrolase that is also encountered in eucarya. In, solution, the S. solfataricus hydrolase behaves as a dimer. In agreement, the crystalline structure of this enzyme indicates the formation of a, dimer. Each protomer is made of a mixed five-stranded beta-sheet, surrounded by two groups of two alpha-helices. The dimer interface is, mainly formed by van der Waals interactions between hydrophobic residues, belonging to the two N-terminal alpha1 helices contributed by two, protomers. Site-directed mutagenesis experiments were designed for probing, the basis of specificity of the archaeal hydrolase. Among the strictly, conserved residues within the archaeal/eucaryal peptidyl-tRNA hydrolase, family, three residues, K18, D86, and T90, appear of utmost importance for, activity. They are located in the N-part of alpha1 and in the beta3-beta4, loop. K18 and D86, which form a salt bridge, might play a role in the, catalysis thanks to their acid and basic functions, whereas the OH group, of T90 could act as a nucleophile. These observations clearly distinguish, the active site of the archaeal/eucaryal hydrolases from that of the, bacterial/eucaryal ones, where a histidine is believed to serve as the, catalytic base.
The 3-D structure of the peptidyl-tRNA hydrolase from the archaea Sulfolobus solfataricus has been solved at 1.8 A resolution. Homologues of this enzyme are found in archaea and eucarya. Bacteria display a different type of peptidyl-tRNA hydrolase that is also encountered in eucarya. In solution, the S. solfataricus hydrolase behaves as a dimer. In agreement, the crystalline structure of this enzyme indicates the formation of a dimer. Each protomer is made of a mixed five-stranded beta-sheet surrounded by two groups of two alpha-helices. The dimer interface is mainly formed by van der Waals interactions between hydrophobic residues belonging to the two N-terminal alpha1 helices contributed by two protomers. Site-directed mutagenesis experiments were designed for probing the basis of specificity of the archaeal hydrolase. Among the strictly conserved residues within the archaeal/eucaryal peptidyl-tRNA hydrolase family, three residues, K18, D86, and T90, appear of utmost importance for activity. They are located in the N-part of alpha1 and in the beta3-beta4 loop. K18 and D86, which form a salt bridge, might play a role in the catalysis thanks to their acid and basic functions, whereas the OH group of T90 could act as a nucleophile. These observations clearly distinguish the active site of the archaeal/eucaryal hydrolases from that of the bacterial/eucaryal ones, where a histidine is believed to serve as the catalytic base.


==About this Structure==
==About this Structure==
1XTY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XTY OCA].  
1XTY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTY OCA].  


==Reference==
==Reference==
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[[Category: mixed beta sheet]]
[[Category: mixed beta sheet]]


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