1ejb

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(New page: 200px<br /><applet load="1ejb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejb, resolution 1.85&Aring;" /> '''LUMAZINE SYNTHASE FR...)
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[[Image:1ejb.jpg|left|200px]]<br /><applet load="1ejb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ejb, resolution 1.85&Aring;" />
caption="1ejb, resolution 1.85&Aring;" />
'''LUMAZINE SYNTHASE FROM SACCHAROMYCES CEREVISIAE'''<br />
'''LUMAZINE SYNTHASE FROM SACCHAROMYCES CEREVISIAE'''<br />
==Overview==
==Overview==
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Lumazine synthase of Saccharomyces cerevisiae is a homopentamer with a, molecular weight of 90 kDa. Crystals of the recombinant enzyme with a size, of up to 1.6 mm were obtained. The space group is P4(1)2(1)2 with lattice, dimensions 82.9 A x 82.9 A x 300.2 A. X-ray diffraction data collected, under cryogenic conditions were complete to 1.85 A resolution. The, structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-p hosphonic, acid was solved via molecular replacement using the structure of the, Bacillus subtilis enzyme as search model and was refined to a final, R-factor of 19.8% (Rfree: 22.5%). The conformation of the active site, ligand of the enzyme mimicks that of the Schiff base intermediate of the, enzyme-catalyzed reaction. The data enable the reconstruction of the, reactant topology during the early steps of the catalytic reaction., Structural determinants, which are likely to be responsible for the, inability of the S. cerevisiae enzyme to form icosahedral capsids, will be, discussed.
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Lumazine synthase of Saccharomyces cerevisiae is a homopentamer with a molecular weight of 90 kDa. Crystals of the recombinant enzyme with a size of up to 1.6 mm were obtained. The space group is P4(1)2(1)2 with lattice dimensions 82.9 A x 82.9 A x 300.2 A. X-ray diffraction data collected under cryogenic conditions were complete to 1.85 A resolution. The structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-p hosphonic acid was solved via molecular replacement using the structure of the Bacillus subtilis enzyme as search model and was refined to a final R-factor of 19.8% (Rfree: 22.5%). The conformation of the active site ligand of the enzyme mimicks that of the Schiff base intermediate of the enzyme-catalyzed reaction. The data enable the reconstruction of the reactant topology during the early steps of the catalytic reaction. Structural determinants, which are likely to be responsible for the inability of the S. cerevisiae enzyme to form icosahedral capsids, will be discussed.
==About this Structure==
==About this Structure==
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1EJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with INJ as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJB OCA].
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1EJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=INJ:'>INJ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJB OCA].
==Reference==
==Reference==
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[[Category: x-ray structure analysis]]
[[Category: x-ray structure analysis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:03:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:24 2008''

Revision as of 10:28, 21 February 2008


1ejb, resolution 1.85Å

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LUMAZINE SYNTHASE FROM SACCHAROMYCES CEREVISIAE

Overview

Lumazine synthase of Saccharomyces cerevisiae is a homopentamer with a molecular weight of 90 kDa. Crystals of the recombinant enzyme with a size of up to 1.6 mm were obtained. The space group is P4(1)2(1)2 with lattice dimensions 82.9 A x 82.9 A x 300.2 A. X-ray diffraction data collected under cryogenic conditions were complete to 1.85 A resolution. The structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-p hosphonic acid was solved via molecular replacement using the structure of the Bacillus subtilis enzyme as search model and was refined to a final R-factor of 19.8% (Rfree: 22.5%). The conformation of the active site ligand of the enzyme mimicks that of the Schiff base intermediate of the enzyme-catalyzed reaction. The data enable the reconstruction of the reactant topology during the early steps of the catalytic reaction. Structural determinants, which are likely to be responsible for the inability of the S. cerevisiae enzyme to form icosahedral capsids, will be discussed.

About this Structure

1EJB is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Riboflavin synthase, with EC number 2.5.1.9 Full crystallographic information is available from OCA.

Reference

The atomic structure of pentameric lumazine synthase from Saccharomyces cerevisiae at 1.85 A resolution reveals the binding mode of a phosphonate intermediate analogue., Meining W, Mortl S, Fischer M, Cushman M, Bacher A, Ladenstein R, J Mol Biol. 2000 May 26;299(1):181-97. PMID:10860731

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