Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti
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Ubiquinol Oxidase in Acetobacter aceti
The terminal oxidase for ethanol oxidation in Acetobacter aced was purified as a complex consisting of four subunits (subunits I, II, III, and IV) with molecular masses of 72, 34, 21, and 13 kDa, respectively. Spectrophotometric analysis and catalytic properties determined with the purified enzyme showed that it belonged to a family of cytochrome a, (ba)-type ubiquinol oxidases. A polymerase ch...
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The crystal structure of the ternary complex of NAD+-dependent formate dehydrogenase from the methylotrophic bacterium Moraxella sp. C-1 with the cofactor (NAD+) and the inhibitor (azide ion) was established at 1.1 A resolution. The complex mimics the structure of the transition state of the enzymatic reaction. The structure was refined with anisotropic displacitalicents parameters for non-hydr...
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The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs ...
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The morphological features of the cell wall, plasma membrane, protoplasmic constituents, and flagella of Acetobacter suboxydans (ATCC 621) were studied by thin sectioning and negative staining. Thin sections of the cell wall demonstrate an outer membrane and an inner, more homogeneous layer. These observations are consistent with those of isolated, gram-negative cell-wall ghosts and the chemica...
متن کاملThe structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
The 1.94 A structure of methanol dehydrogenase has been used to provide a model structure for part of a membrane quinohaemoprotein alcohol dehydrogenase. The basic superbarrel structure and the active-site region are retained, indicating essentially similar mechanisms of action, but there are considerable differences in the external loops, particularly those involved in formation of the shallow...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2006
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.062519707