1bro: Difference between revisions

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==Overview==

The crystal structure of the bromoperoxidase A2 from Streptomyces, aureofaciens (ATCC 10762) has been determined by isomorphous replacement, and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme, catalyzes the bromination of organic compounds in the presence of bromide, and peroxide. The structure confirms the absence of cofactors such as, metal ions or haem groups and shows the general topology of the alpha/beta, hydrolase fold. The active centre is at the end of a deep pocket and, includes a catalytic triad of Ser 98, Asp 228 and His 257. The active, centre is connected by a narrow tunnel to a second pocket on the enzyme, surface.

The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.

==About this Structure==

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[[Category: Streptomyces aureofaciens]]

[[Category: Haag, T.]]

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

[[Category: Hecht, H J.]]

[[Category: Pee, K.H.Van.]]

[[Category: Pee, K H.Van.]]

[[Category: Pfeifer, O.]]

[[Category: Sobek, H.]]

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[[Category: peroxidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 09~~:33:43 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:20 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of the bromoperoxidase A2 from Streptomyces, aureofaciens (ATCC 10762) has been determined by isomorphous replacement, and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme, catalyzes the bromination of organic compounds in the presence of bromide, and peroxide. The structure confirms the absence of cofactors such as, metal ions or haem groups and shows the general topology of the alpha/beta, hydrolase fold. The active centre is at the end of a deep pocket and, includes a catalytic triad of Ser 98, Asp 228 and His 257. The active, centre is connected by a narrow tunnel to a second pocket on the enzyme, surface.
+The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Streptomyces aureofaciens]]
 [[Category: Haag, T.]]
-[[Category: Hecht, H.J.]]
+[[Category: Hecht, H J.]]
-[[Category: Pee, K.H.Van.]]
+[[Category: Pee, K H.Van.]]
 [[Category: Pfeifer, O.]]
 [[Category: Sobek, H.]]
@@ Line 24: / Line 24: @@
 [[Category: peroxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:33:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:20 2008''