2ayt: Difference between revisions

Revision as of 17:32, 21 February 2008

The crystal structure of a protein disulfide oxidoreductase from aquifex aeolicus

OverviewOverview

A potential role in disulfide bond formation in the intracellular proteins of thermophilic organisms has recently been attributed to a new family of protein disulfide isomerase (PDI)-like proteins. Members of this family are characterized by a molecular mass of about 26kDa and by two Trx folds, each comprising a CXXC active site motif. We report on the functional and structural characterization of a new member of this family, which was isolated from the thermophilic bacterium Aquifex aeolicus (AaPDO). Functional studies have revealed the high catalytic efficiency of this enzyme in reducing, oxidizing and isomerizing disulfide bridges. Site-directed mutagenesis experiments have suggested that its two active sites have similar functional properties, i.e. that each of them imparts partial activity to the enzyme. This similarity was confirmed by the analysis of the enzyme crystal structure, which points to similar geometrical parameters and solvent accessibilities for the two active sites. The results demonstrated that AaPDO is the most PDI-like of all prokaryotic proteins so far known. Thus, further experimental studies on this enzyme are likely to provide important information on the eukaryotic homologue.

About this StructureAbout this Structure

2AYT is a Single protein structure of sequence from Aquifex aeolicus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus., Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S, J Mol Biol. 2006 Feb 10;356(1):155-64. Epub 2005 Dec 1. PMID:16364362

Page seeded by OCA on Thu Feb 21 16:32:25 2008

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 ==Overview==
-A potential role in disulfide bond formation in the intracellular proteins, of thermophilic organisms has recently been attributed to a new family of, protein disulfide isomerase (PDI)-like proteins. Members of this family, are characterized by a molecular mass of about 26kDa and by two Trx folds, each comprising a CXXC active site motif. We report on the functional and, structural characterization of a new member of this family, which was, isolated from the thermophilic bacterium Aquifex aeolicus (AaPDO)., Functional studies have revealed the high catalytic efficiency of this, enzyme in reducing, oxidizing and isomerizing disulfide bridges., Site-directed mutagenesis experiments have suggested that its two active, sites have similar functional properties, i.e. that each of them imparts, partial activity to the enzyme. This similarity was confirmed by the, analysis of the enzyme crystal structure, which points to similar, geometrical parameters and solvent accessibilities for the two active, sites. The results demonstrated that AaPDO is the most PDI-like of all, prokaryotic proteins so far known. Thus, further experimental studies on, this enzyme are likely to provide important information on the eukaryotic, homologue.
+A potential role in disulfide bond formation in the intracellular proteins of thermophilic organisms has recently been attributed to a new family of protein disulfide isomerase (PDI)-like proteins. Members of this family are characterized by a molecular mass of about 26kDa and by two Trx folds, each comprising a CXXC active site motif. We report on the functional and structural characterization of a new member of this family, which was isolated from the thermophilic bacterium Aquifex aeolicus (AaPDO). Functional studies have revealed the high catalytic efficiency of this enzyme in reducing, oxidizing and isomerizing disulfide bridges. Site-directed mutagenesis experiments have suggested that its two active sites have similar functional properties, i.e. that each of them imparts partial activity to the enzyme. This similarity was confirmed by the analysis of the enzyme crystal structure, which points to similar geometrical parameters and solvent accessibilities for the two active sites. The results demonstrated that AaPDO is the most PDI-like of all prokaryotic proteins so far known. Thus, further experimental studies on this enzyme are likely to provide important information on the eukaryotic homologue.
 ==About this Structure==
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 [[Category: Aquifex aeolicus]]
 [[Category: Single protein]]
-[[Category: Ambrosio, K.D.]]
+[[Category: Ambrosio, K D.]]
 [[Category: Bartolucci, S.]]
 [[Category: Pedone, C.]]
 [[Category: Pedone, E.]]
 [[Category: Rossi, M.]]
-[[Category: Simone, G.De.]]
+[[Category: Simone, G De.]]
 [[Category: GOL]]
 [[Category: SO4]]
@@ Line 25: / Line 25: @@
 [[Category: thioredoxin fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:12:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:25 2008''