Literature DB >> 22949195

Preliminary X-ray crystallographic analysis of α-carbonic anhydrase from Thiomicrospira crunogena XCL-2.

Natalia Díaz Torres1, Guillermo González, Shyamasri Biswas, Kathleen M Scott, Robert McKenna.   

Abstract

Thiomicrospira crunogena XCL-2 is a novel sulfur-oxidizing chemolithoautotroph that plays a significant role in the sustainability of deep-sea hydrothermal vent communities. This recently discovered gammaproteobacterium encodes and expresses four carbonic anhydrases (CAs) from three evolutionarily and structurally distinct CA families: an α-CA, two β-CAs and a γ-CA. In order to characterize and elucidate the physiological roles of these CAs, X-ray crystallographic structural studies have been initiated on the α-CA. The α-CA crystallized in space group C2. The crystals diffracted to a maximum resolution of 2.6 Å, with unit-cell parameters a = 127.1, b = 102.2, c = 105.0 Å, β = 127.3°, and a calculated Matthews coefficient of 2.04 Å(3) Da(-1) with four identical protein molecules in the crystallographic asymmetric unit. A preliminary solution was determined by molecular replacement with the PHENIX AutoMR wizard, which had an initial TFZ score of 17.9. Refinement of the structure is currently in progress.

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Year:  2012        PMID: 22949195      PMCID: PMC3433198          DOI: 10.1107/S1744309112031053

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


  16 in total

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  1 in total

1.  Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration.

Authors:  Natalia A Díaz-Torres; Brian P Mahon; Christopher D Boone; Melissa A Pinard; Chingkuang Tu; Robert Ng; Mavis Agbandje-McKenna; David Silverman; Kathleen Scott; Robert McKenna
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2015-07-31
  1 in total

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