1h13

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[[Category: xylan degradation]]
[[Category: xylan degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:07:20 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:25:12 2007''

Revision as of 13:20, 30 October 2007


1h13, resolution 1.30Å

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STRUCTURE OF A COLD-ADAPTED FAMILY 8 XYLANASE

Overview

Enzymes from psychrophilic organisms differ from their mesophilic, counterparts in having a lower thermostability and a higher specific, activity at low and moderate temperatures. The current consensus is that, they have an increased flexibility, enhancing accommodation and, transformation of the substrates at low energy costs. Here we describe the, structure of the xylanase from the Antarctic bacterium Pseudoalteromonas, haloplanktis at 1.3 A resolution. Xylanases are usually grouped into, glycosyl hydrolase families 10 and 11, but this enzyme belongs to family, 8. The fold differs from that of other known xylanases and can be, described as an (alpha/alpha)(6) barrel. Various parameters that may, explain the cold-adapted properties were examined and indicated that the, protein has a ... [(full description)]

About this Structure

1H13 is a [Single protein] structure of sequence from [Pseudoalteromonas haloplanktis]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

The structure of a cold-adapted family 8 xylanase at 1.3 A resolution. Structural adaptations to cold and investgation of the active site., Van Petegem F, Collins T, Meuwis MA, Gerday C, Feller G, Van Beeumen J, J Biol Chem. 2003 Feb 28;278(9):7531-9. Epub 2002 Dec 9. PMID:12475991

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