1dbf
From Proteopedia
(New page: 200px<br /><applet load="1dbf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dbf, resolution 1.30Å" /> '''CHORISMATE MUTASE FR...) |
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| - | [[Image:1dbf.gif|left|200px]]<br /><applet load="1dbf" size=" | + | [[Image:1dbf.gif|left|200px]]<br /><applet load="1dbf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dbf, resolution 1.30Å" /> | caption="1dbf, resolution 1.30Å" /> | ||
'''CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM'''<br /> | '''CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the Bacillus subtilis chorismate mutase, an | + | The crystal structure of the Bacillus subtilis chorismate mutase, an enzyme of the aromatic amino acids biosynthetic pathway, was determined to 1.30 A resolution. The structure of the homotrimer was determined by molecular replacement using orthorhombic crystals of space group P2(1)2(1)2(1) with unit-cell parameters a = 52.2, b = 83. 8, c = 86.0 A. The ABC trimer of the monoclinic crystal structure [Chook et al. (1994), J. Mol. Biol. 240, 476-500] was used as the starting model. The final coordinates are composed of three complete polypeptide chains of 127 amino-acid residues. In addition, there are nine sulfate ions, five glycerol molecules and 424 water molecules clearly visible in the structure. This structure was refined with aniosotropic temperature factors, has excellent geometry and a crystallographic R factor of 0.169 with an R(free) of 0.236. The three active sites of the macromolecule are at the subunit interfaces, with residues from two subunits contributing to each site. This orthorhombic crystal form was grown using ammonium sulfate as the precipitant; glycerol was used as a cryoprotectant during data collection. A glycerol molecule and sulfate ion in each of the active sites was found mimicking a transition-state analog. In this structure, the C-terminal tails of the subunits of the trimer are hydrogen bonded to residues of the active site of neighboring trimers in the crystal and thus cross-link the molecules in the crystal lattice. |
==About this Structure== | ==About this Structure== | ||
| - | 1DBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] Full crystallographic information is available from [http:// | + | 1DBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chorismate mutase]] | [[Category: Chorismate mutase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gilliland, G | + | [[Category: Gilliland, G L.]] |
| - | [[Category: Ladner, J | + | [[Category: Ladner, J E.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: shikimate pathway]] | [[Category: shikimate pathway]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:52 2008'' |
Revision as of 10:14, 21 February 2008
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CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM
Overview
The crystal structure of the Bacillus subtilis chorismate mutase, an enzyme of the aromatic amino acids biosynthetic pathway, was determined to 1.30 A resolution. The structure of the homotrimer was determined by molecular replacement using orthorhombic crystals of space group P2(1)2(1)2(1) with unit-cell parameters a = 52.2, b = 83. 8, c = 86.0 A. The ABC trimer of the monoclinic crystal structure [Chook et al. (1994), J. Mol. Biol. 240, 476-500] was used as the starting model. The final coordinates are composed of three complete polypeptide chains of 127 amino-acid residues. In addition, there are nine sulfate ions, five glycerol molecules and 424 water molecules clearly visible in the structure. This structure was refined with aniosotropic temperature factors, has excellent geometry and a crystallographic R factor of 0.169 with an R(free) of 0.236. The three active sites of the macromolecule are at the subunit interfaces, with residues from two subunits contributing to each site. This orthorhombic crystal form was grown using ammonium sulfate as the precipitant; glycerol was used as a cryoprotectant during data collection. A glycerol molecule and sulfate ion in each of the active sites was found mimicking a transition-state analog. In this structure, the C-terminal tails of the subunits of the trimer are hydrogen bonded to residues of the active site of neighboring trimers in the crystal and thus cross-link the molecules in the crystal lattice.
About this Structure
1DBF is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Chorismate mutase, with EC number 5.4.99.5 Full crystallographic information is available from OCA.
Reference
The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer., Ladner JE, Reddy P, Davis A, Tordova M, Howard AJ, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):673-83. PMID:10818343
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