Structure of Phaseolin at 2·2 Å Resolution

Lawrence, Michael C.; Izard, Tina; Beuchat, M.; Blagrove, R.J.; Colman, P.M.

doi:10.1006/jmbi.1994.1333

Cited by 234 publications

(135 citation statements)

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“…Conserved histidine and glutamic acid residues are indicated by asterisks. The designation of the six strands (C^H) is according to the notation developed for the vicilin phaseolin [18]. Regions of motifs 1 and 2 of the cupin domain are also indicated above.…”

Section: Catalytic Properties Of the Recombinant Tlpgimentioning

confidence: 99%

Characterization of the cupin‐type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralisa

Jeong¹,

Fushinobu²,

Ito³

et al. 2003

FEBS Letters

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The gene encoding phosphoglucose isomerase was cloned from Thermococcus litoralis, and functionally expressed in Escherichia coli. The puri¢ed enzyme, a homodimer of 21.5 kDa subunits, was biochemically characterized. The inhibition constants for four competitive inhibitors were determined. The enzyme contained 1.25 mol Fe and 0.24 mol Zn per dimer. The activity was enhanced by the addition of Fe , but inhibited by Zn 2+ and EDTA. Enzymes with mutations in conserved histidine and glutamate residues in their cupin motifs contained no metals, and showed large decreases in k cat . The circular dichroism spectra of the mutant enzymes and the wild type enzyme were essentially the same but with slight di¡erences.

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Section: Catalytic Properties Of the Recombinant Tlpgimentioning

confidence: 99%

Characterization of the cupin‐type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralisa

Jeong¹,

Fushinobu²,

Ito³

et al. 2003

FEBS Letters

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“…13 15) In addition, digestion of vicilin-type storage proteins by various exogenous proteases generated limited-proteolytic fragments with similar size to that of c30. 24) These findings support the idea that junctional regions are susceptible to proteolysis as occur in steps I and II.…”

Section: F3-conglycinin Degradation During Germination and Seedling Gmentioning

confidence: 99%

Characterization of 30-kDa Fragments Derived from β-Conglycinin Degradation Process during Germination and Seedling Growth of Soybean

Kawai

Suzuki

Asano

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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“…The extensions are partly caused by polyglutamate stretches which are also present in the VRI of legumins from Cupressaceae and Pinaceae [31, 301, suggesting them as a diagnostic feature of conifer legumins. In contrast, the VRI of angiosperm legumins tend to be rich in glutamine, whereas glutamate repeats are preferentially located in the HVR (comprehensive comparison of sequences is given in [36]). Assuming a functional or structural significance inherent to VRI glutamate repeats of conifer legumins, those in the HVR of angiosperm legumins may be viewed as analogous in terms of convergent evolution.…”

Section: % F K T N P N S M V S H I a G K S S I F R L P N D V L A N A mentioning

confidence: 99%

Two Ways of Legumin‐Precursor Processing in Conifers

Häger

Wind

1997

European Journal of Biochemistry

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Subunit monomers and oligomers of crystalloid-type legumins are major components of SDS-soluble fractions from Metasequoia glyptostroboides (Dawn redwood, Taxodiaceae) seed proteins. The subunits are made up of disulfide linked a-polypeptides and p-polypeptides with molecular masses of 33 kDa and 23 -25 kDa, respectively. Unusually for legumins, those from Metasequoia are glycosylated and the carbohydrate moieties are residing in the C-terminal region of the respective P-polypeptides. A Metasequoia endosperm cDNA library has been constructed and legumin-encoding transcripts representing two divergent gene subfamilies have been characterized. Intersubfamily comparisons reveal 75 % identity at the amino acid level and the values range from 53-34% when the legumin precursors deduced were compared with those from angiosperms. The predicted sequences together with data from amino acid sequencing prove that post-translational processing of Metasequoia prolegumins is directed to two different processing sites, each of them specific for one of the legumin subfamilies. The sites involved differ in their relative position and in the junction to be cleaved: Metasequoia legumin precursors MgLegl8 and MgLeg26 contain the conventional post-translational Asn-Gly processing site, which is generally regarded as highly conserved. In contrast, the MgLeg4 precursor is lacking this site and post-translational cleavage is directed to an unusual Asn-Thr processing site located in its hypervariable region, causing Nterminal extension of the /I-polypeptide relative to those hitherto known. Evidence is given that the unusual variant of processing also occurs in other conifers. Phylogenetic analysis reveals the precursors concerned as representatives of a distinct legumin subfamily, originating from duplication of an ancestral gene prior to or at the beginning of Taxodiaceae diversification.Keywords : seed storage protein ; legumin ; post-translational processing ; Metasequoia ; gymnosperms.Legumins are the most widely distributed seed storage proteins in angiosperms and their structure, biosynthesis and intracellular transfer are well conserved throughout the species investigated [l -41. They are synthesized as prepro-type precursors which are cotranslationally transported into the endoplasmic reticulum with the simultaneous cleavage of N-terminal signal peptides. Conversion of prolegumins into their mature forms involves further cleavage, taking place in the vacuole and catalyzed by specific proteases. The most invariable characteristic of known prolegumins is the site where cleavage occurs to form the mature a-polypeptides (~4 0 kDa) and /I-polypeptides (~2 0 kDa), which remain paired by a disulfide bond: with only a few exceptions cleavage is regularly directed to an Asn-Gly junction, and the position of this site is absolutely invariant in all prolegumins known; this pattern of processing has been viewed as highly conserved during evolution [5 -91. However, recent in vitro studies prove that the maturation proteases involved are sign...

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Structure of Phaseolin at 2·2 Å Resolution

Cited by 234 publications

References 0 publications

Characterization of the cupin‐type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralisa

Characterization of the cupin‐type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralisa

Characterization of 30-kDa Fragments Derived from β-Conglycinin Degradation Process during Germination and Seedling Growth of Soybean

Two Ways of Legumin‐Precursor Processing in Conifers

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