1q7s: Difference between revisions
New page: left|200px<br /> <applet load="1q7s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q7s, resolution 2.00Å" /> '''Crystal structure o... |
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'''Crystal structure of bit1'''<br /> | '''Crystal structure of bit1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1Q7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1Q7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7S OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: apoptosis]] | [[Category: apoptosis]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:42:57 2008'' | ||
Revision as of 17:42, 15 February 2008
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Crystal structure of bit1
OverviewOverview
Peptidyl-tRNA hydrolase (Pth) activity releases tRNA from the premature, translation termination product peptidyl-tRNA. Two different enzymes have, been reported to encode such activity, Pth present in bacteria and, eukaryotes and Pth2 present in archaea and eukaryotes. Here we report the, crystallographic structure of the Homo sapiens Pth2 at a 2.0-A resolution, as well as its catalytic properties. In contrast to the structure of, Escherichia coli Pth, H. sapiens Pth2 has an alpha/beta fold with a, four-stranded antiparallel beta-sheet in its core surrounded by two, alpha-helices on each side. This arrangement of secondary structure, elements generates a fold not previously reported. Its catalytic, efficiency is comparable with that reported for the archaeal Sulfolobus, solfataricus Pth2 and higher than that of the bacterial E. coli Pth., Several lines of evidence target the active site to two close loops with, highly conserved residues. This active site architecture is unrelated to, that of E. coli Pth. In addition, intermolecular contacts in the crystal, asymmetric unit cell suggest a likely surface for protein-protein, interactions related to the Pth2-mediated apoptosis.
About this StructureAbout this Structure
1Q7S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity., De Pereda JM, Waas WF, Jan Y, Ruoslahti E, Schimmel P, Pascual J, J Biol Chem. 2004 Feb 27;279(9):8111-5. Epub 2003 Dec 5. PMID:14660562
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