2o9x: Difference between revisions

Revision as of 19:16, 21 February 2008

Crystal Structure Of A Putative Redox Enzyme Maturation Protein From Archaeoglobus Fulgidus

OverviewOverview

This paper describes the crystal structure of AF0173, a putative redox-enzyme maturation protein (REMP) from Archaeoglobus fulgidus. The REMPs serve as chaperones in the maturation of extracytoplasmic oxidoreductases in archaea and bacteria. The all-helical subunits of AF0173 form a dimer arising from the interaction of residues located in a funnel-shaped cavity on one subunit surface with an uncut expression tag from the other subunit. This cavity is likely to represent a binding site for the twin-arginine motif that interacts with REMPs. The conservation of the overall fold in AF0173 and bacterial REMPs as well as the presence of conserved residues in their putative binding sites indicates that REMPs act in a similar manner in archaea and bacteria despite their limited sequence similarity. A model of the binding of the twin-arginine motif by AF0173 is suggested. The solution of the AF0173 structure by the single anomalous dispersion method represents an extreme case of SAD structure determination: low resolution (3.4 A), the absence of NCS and the presence of only two anomalously scattering atoms in the asymmetric unit. An unusually high solvent content (73%) turned out to be important for the success of the density-modification procedures.

About this StructureAbout this Structure

2O9X is a Single protein structure of sequence from Archaeoglobus fulgidus. This structure supersedes the now removed PDB entry 1ZE0. Full crystallographic information is available from OCA.

ReferenceReference

An extremely SAD case: structure of a putative redox-enzyme maturation protein from Archaeoglobus fulgidus at 3.4 A resolution., Kirillova O, Chruszcz M, Shumilin IA, Skarina T, Gorodichtchenskaia E, Cymborowski M, Savchenko A, Edwards A, Minor W, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):348-54. Epub 2007, Feb 21. PMID:17327672

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 ==Overview==
-This paper describes the crystal structure of AF0173, a putative, redox-enzyme maturation protein (REMP) from Archaeoglobus fulgidus. The, REMPs serve as chaperones in the maturation of extracytoplasmic, oxidoreductases in archaea and bacteria. The all-helical subunits of, AF0173 form a dimer arising from the interaction of residues located in a, funnel-shaped cavity on one subunit surface with an uncut expression tag, from the other subunit. This cavity is likely to represent a binding site, for the twin-arginine motif that interacts with REMPs. The conservation of, the overall fold in AF0173 and bacterial REMPs as well as the presence of, conserved residues in their putative binding sites indicates that REMPs, act in a similar manner in archaea and bacteria despite their limited, sequence similarity. A model of the binding of the twin-arginine motif by, AF0173 is suggested. The solution of the AF0173 structure by the single, anomalous dispersion method represents an extreme case of SAD structure, determination: low resolution (3.4 A), the absence of NCS and the presence, of only two anomalously scattering atoms in the asymmetric unit. An, unusually high solvent content (73%) turned out to be important for the, success of the density-modification procedures.
+This paper describes the crystal structure of AF0173, a putative redox-enzyme maturation protein (REMP) from Archaeoglobus fulgidus. The REMPs serve as chaperones in the maturation of extracytoplasmic oxidoreductases in archaea and bacteria. The all-helical subunits of AF0173 form a dimer arising from the interaction of residues located in a funnel-shaped cavity on one subunit surface with an uncut expression tag from the other subunit. This cavity is likely to represent a binding site for the twin-arginine motif that interacts with REMPs. The conservation of the overall fold in AF0173 and bacterial REMPs as well as the presence of conserved residues in their putative binding sites indicates that REMPs act in a similar manner in archaea and bacteria despite their limited sequence similarity. A model of the binding of the twin-arginine motif by AF0173 is suggested. The solution of the AF0173 structure by the single anomalous dispersion method represents an extreme case of SAD structure determination: low resolution (3.4 A), the absence of NCS and the presence of only two anomalously scattering atoms in the asymmetric unit. An unusually high solvent content (73%) turned out to be important for the success of the density-modification procedures.
 ==About this Structure==
-O9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure superseeds the now removed PDB entry 1ZE0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9X OCA].
+O9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entry 1ZE0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9X OCA].
 ==Reference==
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 [[Category: Gorodichtchenskaia, E.]]
 [[Category: Kirillova, O.]]
-[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
+[[Category: MCSG, Midwest Center for Structural Genomics.]]
 [[Category: Minor, W.]]
 [[Category: Savchenko, A.]]
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 [[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:56:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:09 2008''