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(New page: 200px<br /> <applet load="1ogo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ogo, resolution 1.65&Aring;" /> '''DEX49A FROM PENICIL...)
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==About this Structure==
==About this Structure==
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1OGO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]].
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1OGO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]]. Active as [[http://en.wikipedia.org/wiki/Dextranase Dextranase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]].
==Reference==
==Reference==
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962629 12962629]
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962629 12962629]
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[[Category: Dextranase]]
[[Category: Penicillium minioluteum]]
[[Category: Penicillium minioluteum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:15:23 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:54:57 2007''

Revision as of 11:50, 30 October 2007


1ogo, resolution 1.65Å

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DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE

Overview

Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, ... [(full description)]

About this Structure

1OGO is a [Single protein] structure of sequence from [Penicillium minioluteum]. Active as [Dextranase], with EC number [3.2.1.11]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:12962629

Page seeded by OCA on Tue Oct 30 13:54:57 2007

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