1zjb: Difference between revisions

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Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (monoclinic form)

OverviewOverview

The trehalulose synthase (MutB) from Pseudomonas mesoacidophila MX-45, belonging to glycoside hydrolase family 13, catalyses the isomerization of sucrose to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as main products and glucose and fructose in residual amounts from the hydrolytic reaction. To date, a three-dimensional structure of a sucrose isomerase that produces mainly trehalulose, as is the case for MutB, has been lacking. Crystallographic studies of this 64 kDa enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of sucrose decomposition, isomerization and of the selectivity of this enzyme that leads to the formation of different products. The MutB protein has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. Two different crystal forms have been obtained: one diffracts X-rays to 1.6 A resolution using synchrotron radiation and belongs to space group P1, with unit-cell parameters a = 63.8, b = 72.0, c = 82.2 A, alpha = 67.5, beta = 73.1, gamma = 70.8 degrees, while the other form diffracts to 1.8 A resolution using synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 63.7, b = 85.9, c = 119.7 A, beta = 97.7 degrees. A molecular-replacement solution has been found using the structure of the isomaltulose synthase (PalI) from Klebsiella sp. LX3 as a search model.

About this StructureAbout this Structure

1ZJB is a Single protein structure of sequence from Pseudomonas mesoacidophila with and as ligands. Active as Isomaltulose synthase, with EC number 5.4.99.11 Full crystallographic information is available from OCA.

ReferenceReference

Expression, purification, crystallization and preliminary X-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45., Ravaud S, Watzlawick H, Haser R, Mattes R, Aghajari N, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):100-3. Epub 2004 Dec 2. PMID:16508103

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-[[Image:1zjb.gif|left|200px]]<br /><applet load="1zjb" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1zjb, resolution 1.80&Aring;" />
 '''Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 (monoclinic form)'''<br />
 ==Overview==
-The trehalulose synthase (MutB) from Pseudomonas mesoacidophila MX-45, belonging to glycoside hydrolase family 13, catalyses the isomerization of, sucrose to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose), and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as main, products and glucose and fructose in residual amounts from the hydrolytic, reaction. To date, a three-dimensional structure of a sucrose isomerase, that produces mainly trehalulose, as is the case for MutB, has been, lacking. Crystallographic studies of this 64 kDa enzyme have therefore, been initiated in order to contribute to the understanding of the, molecular basis of sucrose decomposition, isomerization and of the, selectivity of this enzyme that leads to the formation of different, products. The MutB protein has been overexpressed, purified and, crystallized using the hanging-drop vapour-diffusion method. Two different, crystal forms have been obtained: one diffracts X-rays to 1.6 A resolution, using synchrotron radiation and belongs to space group P1, with unit-cell, parameters a = 63.8, b = 72.0, c = 82.2 A, alpha = 67.5, beta = 73.1, gamma = 70.8 degrees, while the other form diffracts to 1.8 A resolution, using synchrotron radiation and belongs to space group P2(1), with, unit-cell parameters a = 63.7, b = 85.9, c = 119.7 A, beta = 97.7 degrees., A molecular-replacement solution has been found using the structure of the, isomaltulose synthase (PalI) from Klebsiella sp. LX3 as a search model.
+The trehalulose synthase (MutB) from Pseudomonas mesoacidophila MX-45, belonging to glycoside hydrolase family 13, catalyses the isomerization of sucrose to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as main products and glucose and fructose in residual amounts from the hydrolytic reaction. To date, a three-dimensional structure of a sucrose isomerase that produces mainly trehalulose, as is the case for MutB, has been lacking. Crystallographic studies of this 64 kDa enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of sucrose decomposition, isomerization and of the selectivity of this enzyme that leads to the formation of different products. The MutB protein has been overexpressed, purified and crystallized using the hanging-drop vapour-diffusion method. Two different crystal forms have been obtained: one diffracts X-rays to 1.6 A resolution using synchrotron radiation and belongs to space group P1, with unit-cell parameters a = 63.8, b = 72.0, c = 82.2 A, alpha = 67.5, beta = 73.1, gamma = 70.8 degrees, while the other form diffracts to 1.8 A resolution using synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 63.7, b = 85.9, c = 119.7 A, beta = 97.7 degrees. A molecular-replacement solution has been found using the structure of the isomaltulose synthase (PalI) from Klebsiella sp. LX3 as a search model.
 ==About this Structure==
-ZJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mesoacidophila Pseudomonas mesoacidophila] with CA and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isomaltulose_synthase Isomaltulose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.11 5.4.99.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZJB OCA].
+ZJB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mesoacidophila Pseudomonas mesoacidophila] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isomaltulose_synthase Isomaltulose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.11 5.4.99.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZJB OCA].
 ==Reference==
-Expression, purification, crystallization and preliminary X-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45., Ravaud S, Watzlawick H, Haser R, Mattes R, Aghajari N, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):100-3. Epub 2004 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16508103 16508103]
+Expression, purification, crystallization and preliminary X-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45., Ravaud S, Watzlawick H, Haser R, Mattes R, Aghajari N, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):100-3. Epub 2004 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16508103 16508103]
 [[Category: Isomaltulose synthase]]
 [[Category: Pseudomonas mesoacidophila]]
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 [[Category: trehalulose synthase]]
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