Literature DB >> 20516588

The 1.4 A resolution structure of Paracoccus pantotrophus pseudoazurin.

Shabir Najmudin1, Sofia R Pauleta, Isabel Moura, Maria J Romão.   

Abstract

Pseudoazurins are small type 1 copper proteins that are involved in the flow of electrons between various electron donors and acceptors in the bacterial periplasm, mostly under denitrifying conditions. The previously determined structure of Paracoccus pantotrophus pseudoazurin in the oxidized form was improved to a nominal resolution of 1.4 A, with R and R(free) values of 0.188 and 0.206, respectively. This high-resolution structure makes it possible to analyze the interactions between the monomers and the solvent structure in detail. Analysis of the high-resolution structure revealed the structural regions that are responsible for monomer-monomer recognition during dimer formation and for protein-protein interaction and that are important for partner recognition. The pseudoazurin structure was compared with other structures of various type 1 copper proteins and these were grouped into families according to similarities in their secondary structure; this may be useful in the annotation of copper proteins in newly sequenced genomes and in the identification of novel copper proteins.

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Year:  2010        PMID: 20516588      PMCID: PMC2882758          DOI: 10.1107/S1744309110013989

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  52 in total

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Authors:  G S Thompson; Y C Leung; S J Ferguson; S E Radford; C Redfield
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Authors:  Loretta M Murphy; Fraser E Dodd; Faridoon K Yousafzai; Robert R Eady; S Samar Hasnain
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5.  Solvent content of protein crystals.

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6.  NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential.

Authors:  M V Botuyan; A Toy-Palmer; J Chung; R C Blake; P Beroza; D A Case; H J Dyson
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Review 7.  Copper protein structures.

Authors:  E T Adman
Journal:  Adv Protein Chem       Date:  1991

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7.  CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential.

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