1bro

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Streptomyces aureofaciens]]
[[Category: Streptomyces aureofaciens]]
[[Category: Haag, T.]]
[[Category: Haag, T.]]
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[[Category: Hecht, H.J.]]
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[[Category: Hecht, H J.]]
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[[Category: Pee, K.H.Van.]]
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[[Category: Pee, K H.Van.]]
[[Category: Pfeifer, O.]]
[[Category: Pfeifer, O.]]
[[Category: Sobek, H.]]
[[Category: Sobek, H.]]
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[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:20 2008''

Revision as of 09:58, 21 February 2008


1bro, resolution 2.05Å

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BROMOPEROXIDASE A2

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.

About this Structure

1BRO is a Single protein structure of sequence from Streptomyces aureofaciens. Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold., Hecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH, Nat Struct Biol. 1994 Aug;1(8):532-7. PMID:7664081

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