1ofn: Difference between revisions

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==Overview==

The vancomycin class of antibiotics is regarded as the last line of, defence against Gram-positive bacteria. The compounds used clinically are, very complex organic molecules and are made by fermentation. The, biosynthesis of these is complex and fascinating. Its study holds out the, prospect of utilizing genetic engineering of the enzymes in the pathway in, order to produce novel vancomycin analogues. In part, this requires, detailed structural insight into substrate specificity as well as the, enzyme mechanism. The crystallization of one of the enzymes in the, chloroeremomycin biosynthetic pathway (a member of the vancomycin family), dTDP-3-amino-4-keto 2,3,6-trideoxy-3-C-methyl-glucose-5-epimerase (EvaD), from Amycolatopsis orientalis, is reported here. The protein is fourth in, the pathway which makes a carbohydrate essential for the activity of, chloroeremomycin. The crystals of EvaD diffract to 1.5 A and have, unit-cell parameters a = 98.6, b = 72.0, c = 57.1 A with space group, P2(1)2(1)2. Data to this resolution were collected at the European, Synchrotron Radiation Facility.

The vancomycin class of antibiotics is regarded as the last line of defence against Gram-positive bacteria. The compounds used clinically are very complex organic molecules and are made by fermentation. The biosynthesis of these is complex and fascinating. Its study holds out the prospect of utilizing genetic engineering of the enzymes in the pathway in order to produce novel vancomycin analogues. In part, this requires detailed structural insight into substrate specificity as well as the enzyme mechanism. The crystallization of one of the enzymes in the chloroeremomycin biosynthetic pathway (a member of the vancomycin family), dTDP-3-amino-4-keto 2,3,6-trideoxy-3-C-methyl-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis, is reported here. The protein is fourth in the pathway which makes a carbohydrate essential for the activity of chloroeremomycin. The crystals of EvaD diffract to 1.5 A and have unit-cell parameters a = 98.6, b = 72.0, c = 57.1 A with space group P2(1)2(1)2. Data to this resolution were collected at the European Synchrotron Radiation Facility.

==About this Structure==

Line 13:

[[Category: Amycolatopsis orientalis]]

[[Category: Single protein]]

[[Category: Merkel, A.B.]]

[[Category: Merkel, A B.]]

[[Category: Naismith, J.H.]]

[[Category: Naismith, J H.]]

[[Category: GOL]]

[[Category: epimerase]]

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[[Category: vancomycin group antibiotic]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The vancomycin class of antibiotics is regarded as the last line of, defence against Gram-positive bacteria. The compounds used clinically are, very complex organic molecules and are made by fermentation. The, biosynthesis of these is complex and fascinating. Its study holds out the, prospect of utilizing genetic engineering of the enzymes in the pathway in, order to produce novel vancomycin analogues. In part, this requires, detailed structural insight into substrate specificity as well as the, enzyme mechanism. The crystallization of one of the enzymes in the, chloroeremomycin biosynthetic pathway (a member of the vancomycin family), dTDP-3-amino-4-keto 2,3,6-trideoxy-3-C-methyl-glucose-5-epimerase (EvaD), from Amycolatopsis orientalis, is reported here. The protein is fourth in, the pathway which makes a carbohydrate essential for the activity of, chloroeremomycin. The crystals of EvaD diffract to 1.5 A and have, unit-cell parameters a = 98.6, b = 72.0, c = 57.1 A with space group, P2(1)2(1)2. Data to this resolution were collected at the European, Synchrotron Radiation Facility.
+The vancomycin class of antibiotics is regarded as the last line of defence against Gram-positive bacteria. The compounds used clinically are very complex organic molecules and are made by fermentation. The biosynthesis of these is complex and fascinating. Its study holds out the prospect of utilizing genetic engineering of the enzymes in the pathway in order to produce novel vancomycin analogues. In part, this requires detailed structural insight into substrate specificity as well as the enzyme mechanism. The crystallization of one of the enzymes in the chloroeremomycin biosynthetic pathway (a member of the vancomycin family), dTDP-3-amino-4-keto 2,3,6-trideoxy-3-C-methyl-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis, is reported here. The protein is fourth in the pathway which makes a carbohydrate essential for the activity of chloroeremomycin. The crystals of EvaD diffract to 1.5 A and have unit-cell parameters a = 98.6, b = 72.0, c = 57.1 A with space group P2(1)2(1)2. Data to this resolution were collected at the European Synchrotron Radiation Facility.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Amycolatopsis orientalis]]
 [[Category: Single protein]]
-[[Category: Merkel, A.B.]]
+[[Category: Merkel, A B.]]
-[[Category: Naismith, J.H.]]
+[[Category: Naismith, J H.]]
 [[Category: GOL]]
 [[Category: epimerase]]
@@ Line 21: / Line 21: @@
 [[Category: vancomycin group antibiotic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:57:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:09 2008''