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| - | [[Image:1xty.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xty| PDB=1xty | SCENE= }} | | {{STRUCTURE_1xty| PDB=1xty | SCENE= }} |
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| - | '''Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase'''
| + | ===Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase=== |
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| - | ==Overview==
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| - | 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 line below this paragraph, {{ABSTRACT_PUBMED_15766258}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15766258 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15766258}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Schmitt, E.]] | | [[Category: Schmitt, E.]] |
| | [[Category: Mixed beta sheet]] | | [[Category: Mixed beta sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:30:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:40:26 2008'' |
Revision as of 13:40, 29 July 2008
Template:STRUCTURE 1xty
Crystal structure of Sulfolobus solfataricus peptidyl-tRNA hydrolase
Template:ABSTRACT PUBMED 15766258
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
Page seeded by OCA on Tue Jul 29 16:40:26 2008
