1v8o: Difference between revisions

Revision as of 12:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v8o.png

Template:STRUCTURE 1v8o

Crystal Structure of PAE2754 from Pyrobaculum aerophilumCrystal Structure of PAE2754 from Pyrobaculum aerophilum

Template:ABSTRACT PUBMED 14734548

About this StructureAbout this Structure

1V8O is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.

ReferenceReference

Distant structural homology leads to the functional characterization of an archaeal PIN domain as an exonuclease., Arcus VL, Backbro K, Roos A, Daniel EL, Baker EN, J Biol Chem. 2004 Apr 16;279(16):16471-8. Epub 2004 Jan 20. PMID:14734548

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of PAE2754 from Pyrobaculum aerophilum'''
+===Crystal Structure of PAE2754 from Pyrobaculum aerophilum===
-==Overview==
+<!--
-Genome sequencing projects have focused attention on the problem of discovering the functions of protein domains that are widely distributed throughout living species but which are, as yet, largely uncharacterized. One such example is the PIN domain, found in eukaryotes, bacteria, and Archaea, and with suggested roles in signaling, RNase editing, and/or nucleotide binding. The first reported crystal structure of a PIN domain (open reading frame PAE2754, derived from the crenarchaeon, Pyrobaculum aerophilum) has been determined to 2.5 A resolution and is presented here. Mapping conserved residues from a multiple sequence alignment onto the structure identifies a putative active site. The discovery of distant structural homology with several exonucleases, including T4 phage RNase H and flap endonuclease (FEN1), further suggests a likely function for PIN domains as Mg2+-dependent exonucleases, a hypothesis that we have confirmed in vitro. The tetrameric structure of PAE2754, with the active sites inside a tunnel, suggests a mechanism for selective cleavage of single-stranded overhangs or flap structures. These results indicate likely DNA or RNA editing roles for prokaryotic PIN domains, which are strikingly numerous in thermophiles, and in organisms such as Mycobacterium tuberculosis. They also support previous hypotheses that eukaryotic PIN domains participate in RNAi and nonsense-mediated RNA degradation.
+The line below this paragraph, {{ABSTRACT_PUBMED_14734548}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14734548 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14734548}}
 ==About this Structure==
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 [[Category: Semet substituted]]
 [[Category: Structural genomic]]
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