Structure of human phosphoserine phosphatase

Peeraer, Yves; Rabijns, A.; Verboven, Christel; Collet, Jean-François; Schaftingen, E. Van; Ranter, Camiel De

doi:10.1107/s0108767302089444

Acta Cryst Sect A

2002

DOI: 10.1107/s0108767302089444

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Structure of human phosphoserine phosphatase

Yves Peeraer¹,

A. Rabijns²,

Christel Verboven³

et al.

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Cited by 6 publications

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“…Furthermore Ca 2+ inhibited the activity measured in the presence of Mg 2+ . The expression, purification, crystallisation and elucidation of the 1.53 Å resolution, Ca 2+ containing crystal structure have been described elsewhere (PDB ID code 1NNL) [4]. The sixfold coordinated Mg 2+ ion present in the active site of HPSP under normal physiological conditions and in previously reported structures of the PSP family, was replaced by a Ca 2+ ion.…”

mentioning

confidence: 99%

“…We constructed trypsin mutants in which the binding pocket is substituted partially or completely by the factor Xa binding pocket and analyzed the effect of the mutations on the binding of dianhydrosugar-based benzamidine inhibitors by measuring their corresponding Ki values. The series of ligands studied (1)(2)(3)(4), is characterized by a common rigid scaffold, the dianhydrohexitoles isosorbide moiety (Fig.1). We also determined the crystal structures of some of the mutant-inhibitor complexes to investigate the adopted binding mode.…”

mentioning

confidence: 99%

“…In particular, 1 interacts with the specific primarily hydrophobic S1 pocket of the enzyme, by means of its R2 substituent. This feature is particularly interesting and guided us to choose others ligands (2)(3)(4) to investigate the property of binding of these compounds with the Trypsin mutant. Successively, to analyse how the binding is influenced by mutations in the binding pocket, the series of ligands will be examined in complex with others trypsin mutants.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Structural studies of FXa-trypsin mutants complexed by dianhydrosugar-based benzamidine inhibitors

Fenza¹,

Heine²,

Vogler³

et al. 2004

Acta Cryst Sect A

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confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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Structural studies of FXa-trypsin mutants complexed by dianhydrosugar-based benzamidine inhibitors

Fenza¹,

Heine²,

Vogler³

et al. 2004

Acta Cryst Sect A

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“…The different conformation around active sites between yACCD and PH0054 complexes reveals that circumstance around PLP strictly controls enzyme activity. (2). The three enzymes has been cloned from Brassica napus (oilseed rape) and by recombinant E. coli expression, purification, crystallization and structure determination the enzymatic mechanism of the individual enzymes as well as the interaction between the enzymes are being studied.…”

mentioning

confidence: 99%

Structural studies of enzymes involved in peroxisomal β-oxidation

Pedersen¹,

Olsen²,

Bukrinsky³

et al. 2002

Acta Cryst Sect A

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Pectate lyases are the major pectinases that play a key role in the development of the soft-rot disease. Besides in phytopathogens, pectin depolymerization has also been reported in non-pathogenic plant associated bacteria such as the N2fixing endosymbiont Rhizobium and the N2-fixing soil bacterium Azospirillum irakense. A gene from A. irakense encoding a pectate lyase (termed PelA) was isolated by heterologous expression of the gene in Escherichia coli. Analysis of the corresponding amino acid sequence revealed no homology to other bacterial, plant and fungal pectinases leading to the classification of the enzyme in a new pectate lyase family (family 10). The A. irakense PelA has been crystallized using the hanging-drop vapor diffusion method at 277K. These crystals are hexagonal with cell dimensions of a = b = 85.55 Å, c = 230.13 Å, γ = 120°, and space group P6522 having one molecule per asymmetric unit2. Diffraction data to a resolution of 1.97 Å were collected at synchrotron facilities, as well as a three-wavelengths MAD data set on a Hg derivate crystal to a resolution of 2.6 Å. The preliminary structural results show that PelA does not have the characteristic parallel β -helix fold of the polysaccharide pectate lyase families.In higher plants, acc (1-aminocycropropane-1-carboxylate) is a precursor of hormone ethylene that initiates fruit ripening and regulates various processes in growth and development. Several soil microorganisms have acc deaminase, a pyridoxal 5'-phosphate (plp) dependent enzyme, which catalyzes cyclopropane ring opening; the degradation of acc into 2-oxobutyrate and ammonia. Unlike other plp-dependent enzymes, the substrate of this enzyme has no a-hydrogen atom. Thus, a unique mechanism for the bond cleavage is required. In this study, six types of crystal structures have been determined including mutants and homologue protein. Several yACCD (from yeast Hansenula saturnus) mutants lost ACCD activity and were crystallized in the presence of substrate ACC. One of them, K51T made a main absorption band at around 330 nm, and loss of stereospesificity of the reaction to D-and L-serine. The 420 nm absorption was recovered by adding of ACC and structure determination was succeeded at this condition. The structure of yACCD reaction intermediates, K51T-ACC complex shows that PLP rotated to form Schiff base of ACC-PLP. On the other hand, hyperthermophilic archaebacteria Pyrococcus horikoshii OT3 has ACCDhomologue ORF named PH0054 whose amino acid sequence identity is 25% with other ACCD. However, recombinant PH0054 did not show ACCD activity. Crystal structure of PH0054-ACC complex shows similar active site environment with yACCD but a little difference is recognizable. The different conformation around active sites between yACCD and PH0054 complexes reveals that circumstance around PLP strictly controls enzyme activity.Peroxisomal β -oxidation is the predominant pathway of fatty acid breakdown in plants. The β -oxidation is facilitated by three enzymatic steps catalyzed by: Acyl-CoA oxidases (AC...

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“…Psp belongs to a recently identified class of phosphotransferases forming a phosphoaspartate intermediate during catalysis. Crystals of psp were grown in the C2221 space group with 2 molecules in the asymmetric unit [2]. Diffraction data were collected to 1.53 Å and the structure was solved by the MAD method making use of a selenomethionyl derivative.…”

mentioning

confidence: 99%

Reaction intermediates analysis of ACCD and its homologue

Ose¹,

Fujino²,

Yao³

et al. 2002

Acta Cryst Sect A

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Pectate lyases are the major pectinases that play a key role in the development of the soft-rot disease. Besides in phytopathogens, pectin depolymerization has also been reported in non-pathogenic plant associated bacteria such as the N2-fixing endosymbiont Rhizobium and the N2-fixing soil bacterium Azospirillum irakense. A gene from A. irakense encoding a pectate lyase (termed PelA) was isolated by heterologous expression of the gene in Escherichia coli. Analysis of the corresponding amino acid sequence revealed no homology to other bacterial, plant and fungal pectinases leading to the classification of the enzyme in a new pectate lyase family (family 10). The A. irakense PelA has been crystallized using the hanging-drop vapor diffusion method at 277K. These crystals are hexagonal with cell dimensions of a = b = 85.55 Å, c = 230.13 Å, γ = 120°, and space group P6522 having one molecule per asymmetric unit2. Diffraction data to a resolution of 1.97 Å were collected at synchrotron facilities, as well as a three-wavelengths MAD data set on a Hg derivate crystal to a resolution of 2.6 Å. In higher plants, acc (1-aminocycropropane-1-carboxylate) is a precursor of hormone ethylene that initiates fruit ripening and regulates various processes in growth and development. Several soil microorganisms have acc deaminase, a pyridoxal 5'-phosphate (plp) dependent enzyme, which catalyzes cyclopropane ring opening; the degradation of acc into 2-oxobutyrate and ammonia. Unlike other plp-dependent enzymes, the substrate of this enzyme has no a-hydrogen atom. Thus, a unique mechanism for the bond cleavage is required. In this study, six types of crystal structures have been determined including mutants and homologue protein. Several yACCD (from yeast Hansenula saturnus) mutants lost ACCD activity and were crystallized in the presence of substrate ACC. One of them, K51T made a main absorption band at around 330 nm, and loss of stereospesificity of the reaction to D-and L-serine. The 420 nm absorption was recovered by adding of ACC and structure determination was succeeded at this condition. The structure of yACCD reaction intermediates, K51T-ACC complex shows that PLP rotated to form Schiff base of ACC-PLP. On the other hand, hyperthermophilic archaebacteria Pyrococcus horikoshii OT3 has ACCDhomologue ORF named PH0054 whose amino acid sequence identity is 25% with other ACCD. However, recombinant PH0054 did not show ACCD activity. Crystal structure of PH0054-ACC complex shows similar active site environment with yACCD but a little difference is recognizable. The different conformation around active sites between yACCD and PH0054 complexes reveals that circumstance around PLP strictly controls enzyme activity. The existence of ACXs as a family of enzymes that differs in size, subunit composition and substrate specificity (short-, medium-, and long-chain specific) has been demonstrated in several plant species(1). The second step in the β -oxidation is catalyzed by MFE possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenas...

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Structure of human phosphoserine phosphatase

Cited by 6 publications

References 0 publications

Structural studies of FXa-trypsin mutants complexed by dianhydrosugar-based benzamidine inhibitors

Structural studies of FXa-trypsin mutants complexed by dianhydrosugar-based benzamidine inhibitors

Structural studies of enzymes involved in peroxisomal β-oxidation

Reaction intermediates analysis of ACCD and its homologue

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