1xty
From Proteopedia
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| - | [[Image:1xty.gif|left|200px]] | + | [[Image:1xty.gif|left|200px]] |
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| - | '''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase''' | + | {{Structure |
| + | |PDB= 1xty |SIZE=350|CAPTION= <scene name='initialview01'>1xty</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= pth ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XTY is a [ | + | 1XTY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTY OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase., Fromant M, Schmitt E, Mechulam Y, Lazennec C, Plateau P, Blanquet S, Biochemistry. 2005 Mar 22;44(11):4294-301. PMID:[http:// | + | Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase., Fromant M, Schmitt E, Mechulam Y, Lazennec C, Plateau P, Blanquet S, Biochemistry. 2005 Mar 22;44(11):4294-301. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15766258 15766258] |
[[Category: Aminoacyl-tRNA hydrolase]] | [[Category: Aminoacyl-tRNA hydrolase]] | ||
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
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[[Category: mixed beta sheet]] | [[Category: mixed beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:14:29 2008'' |
Revision as of 13:14, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | pth (Pyrococcus abyssi) | ||||||
| Activity: | Aminoacyl-tRNA hydrolase, with EC number 3.1.1.29 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase
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.
About this Structure
1XTY is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase., Fromant M, Schmitt E, Mechulam Y, Lazennec C, Plateau P, Blanquet S, Biochemistry. 2005 Mar 22;44(11):4294-301. PMID:15766258
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