Literature DB >> 8107119

Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Brevibacterium fuscum.

C A Earhart1, R Radhakrishnan, A M Orville, J D Lipscomb, D H Ohlendorf.   

Abstract

The enzyme protocatechuate 3,4-dioxygenase from the Gram positive organism Brevibacterium fuscum crystallizes in the triclinic space group P1 with unit cell dimensions a = 96.1 A, b = 97.2 A, c = 118.1 A and alpha = 113.9 degrees, beta = 90.7 degrees, gamma = 117.8 degrees. The rod-like crystals diffract to 2.4 A resolution. Rotation function analysis suggests that there are six promoters arranged with local 32 symmetry in the asymmetric unit rather than the previously proposed pentameric complex.

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Year:  1994        PMID: 8107119     DOI: 10.1006/jmbi.1994.1143

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.

Authors:  D A D'Argenio; M W Vetting; D H Ohlendorf; L N Ornston
Journal:  J Bacteriol       Date:  1999-10       Impact factor: 3.490

2.  PcaU, a transcriptional activator of genes for protocatechuate utilization in Acinetobacter.

Authors:  U Gerischer; A Segura; L N Ornston
Journal:  J Bacteriol       Date:  1998-03       Impact factor: 3.490

  2 in total

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