Crystal structure of muconolactone isomerase at 3.3 Å resolution

Katti, Suresh; Katz, B.A.; Wyckoff, Harold W.

doi:10.1016/0022-2836(89)90226-x

Cited by 28 publications

(20 citation statements)

References 35 publications

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“…Although these proteins form trimers they are quite different to the type formed by Pn; they do not have an interlocking double /~U3 core structure. Muconolactone isomerase (MI) does have subunits with an interlocking double/3~/~ structure, but this protein forms dodecamers with 52 symmetry (Katti, Katz & Wyckoff, 1989). In addition, the strands of MI form a barrel-like structure with c~-helices on the external surface.…”

Section: Discussionmentioning

confidence: 99%

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 Å

Carr

Cheah²,

Suffolk³

et al. 1996

Acta Cryst D

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Section: Discussionmentioning

confidence: 99%

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 Å

Carr

Cheah²,

Suffolk³

et al. 1996

Acta Cryst D

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“…1): catechol 1,2-dioxygenase (EC 1.13.1.1) (encoded by catA), muconate cycloisomerase (EC 5.5.1.1) (encoded by catB), and muconolactone isomerase (EC 5.3.3.4) (encoded by catC). The P. putida catB and catC nucleotide sequences are of particular interest because they encode proteins for which crystal structures have been determined (14,17). CatC is unusual in that it contains only 97 amino acids in its primary structure, and the five active sites of the enzyme are formed between pairs of protein subunits within a decameric array (17).…”

mentioning

confidence: 99%

“…The P. putida catB and catC nucleotide sequences are of particular interest because they encode proteins for which crystal structures have been determined (14,17). CatC is unusual in that it contains only 97 amino acids in its primary structure, and the five active sites of the enzyme are formed between pairs of protein subunits within a decameric array (17). The three-dimensional structure of CatB (muconate cycloisomerase) proved to be similar to that of MdlA (mandelate racemase), and comparison of the primary structures of these proteins revealed their common ancestry (28).…”

mentioning

confidence: 99%

Discontinuities in the evolution of Pseudomonas putida cat genes

et al. 1995

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The organization and transcriptional control of chromosomal cat genes (required for dissimilation of catechol by the ␤-ketoadipate pathway) in the Pseudomonas putida biotype strain (ATCC 12633) are reported. Nucleotide sequence reveals that catR is separated by 135 bp from the divergently transcribed catBC,A; catC begins 21 nucleotides downstream from catB, and catA begins 41 nucleotides downstream from catC. This contrasts with the gene arrangement in other bacteria, in which catA lies several kilobases upstream from catB. Properties of Tn5 mutants confirmed earlier suggestions that catR is a transcriptional activator and indicated that catA is activated by CatR independently of its activation of catBC. CatR binds to both a DNA fragment containing the catR-catB intergenic region and another DNA fragment containing catC. Pseudomonas strain RB1 resembles P. putida in some respects. Divergence of the two Pseudomonas chromosomes was revealed as nucleotide substitution of about 10% after alignment of known portions of catR,BC,A. Divergent transcriptional controls are suggested by a cluster of nucleotide sequence modifications in Pseudomonas strain RB1 which disrupt a stem-loop structure directly upstream of catB in the P. putida chromosome. Abrupt divergence of the catR,BC,A nucleotide sequences was achieved during evolution by insertion of an 85-bp palindromic genetic element uniquely positioned downstream from P. putida catR and counterpoised by insertion of a similar palindromic sequence in the Pseudomonas strain RB1 catB-catC intergenic region. Properties of the palindromic genetic element suggest that it may serve functions analogous to those of repetitive extragenic palindromic sequences and enteric repetitive intergenic consensus sequences in enteric bacteria.

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“…The structure of Alcaligenes eutrophus chloromuconate cycloisomerase (CI-MLE) (an ot/,B-barrel enzyme) has been solved by molecular replacement using MLE as the search model (Hoier et al, 1994). Structures for several other enzymes of the ,B-ketoadipate pathway exist: P. aeruginosa protocatechuate 3,4-dioxygenase (a mixed/~-barrel enzyme) (Ohlendorf, Lipscomb & Weber, 1988), P. putida muconolactone isomerase (a unique decameric enzyme) (Katti, Katz & Wyckoff, 1989), and Pseudomonas sp. B13 dienelactone hydrolase (an ot/~ hydrolase fold structure) (Pathak & Ollis, 1990;Ollis et al, 1992).…”

Section: International Union Of Crystallographymentioning

confidence: 99%

Crystallization and preliminary crystallographic analysis of 3-carboxy-cis,cis-muconate lactonizing enzyme from Neurospora crassa

Glumoff

Helin²,

Mazur³

et al. 1996

Acta Cryst D

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Crystals of 3-carboxy-cis,cis-muconate lactonizing enzyme (CMLE; E.C. 5.5.1.5) from Neurospora crassa that diffract to high resolution have been obtained. The crystals belong to the orthorhombic space group P212121 with unit-cell dimensions a = 92.1, b = 159.7, c = 236.6A (at 103 K) and diffract at most to 2,~ resolution. The asymmetric unit of the crystals appears to contain two tetrameric CMLE molecules making up a total of 328 kDa per asymmetric unit. Both cross-linking with glutaraldehyde and cryo-cooling to 103 K have been used to facilitate data collection because the crystals are unstable in the X-ray beam; both techniques extend the crystal lifetime but cryo-cooling, unlike glutaraldehyde cross-linking, does not lower the quality of the diffraction pattern.

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Crystal structure of muconolactone isomerase at 3.3 Å resolution

Cited by 28 publications

References 35 publications

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 Å

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 Å

Discontinuities in the evolution of Pseudomonas putida cat genes

Crystallization and preliminary crystallographic analysis of 3-carboxy-cis,cis-muconate lactonizing enzyme from Neurospora crassa

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