2o9x: Difference between revisions

Revision as of 04:24, 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:2o9x.png

Template:STRUCTURE 2o9x

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

Template:ABSTRACT PUBMED 17327672

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

OCA

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+===Crystal Structure Of A Putative Redox Enzyme Maturation Protein From Archaeoglobus Fulgidus===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17327672}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17327672}}
 ==About this Structure==
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