1obb
From Proteopedia
|  (New page: 200px<br /> <applet load="1obb" size="450" color="white" frame="true" align="right" spinBox="true"  caption="1obb, resolution 1.90Å" /> '''ALPHA-GLUCOSIDASE A...) | |||
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| ==About this Structure== | ==About this Structure== | ||
| - | 1OBB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with MAL and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBB OCA]].  | + | 1OBB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with MAL and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBB OCA]].  | 
| ==Reference== | ==Reference== | ||
| Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12588867 12588867] | Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12588867 12588867] | ||
| + | [[Category: Alpha-glucosidase]] | ||
| [[Category: Single protein]] | [[Category: Single protein]] | ||
| [[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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| [[Category: sulfinic acid]] | [[Category: sulfinic acid]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on  | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:11:51 2007'' | 
Revision as of 09:07, 30 October 2007
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ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+
Overview
Glycoside hydrolase family 4 represents an unusual group of glucosidases, with a requirement for NAD+, divalent metal cations, and reducing, conditions. The family is also unique in its inclusion of both alpha- and, beta-specific enzymes. The alpha-glucosidase A, AglA, from Thermotoga, maritima is a typical glycoside hydrolase family 4 enzyme, requiring NAD+, and Mn2+ as well as strongly reducing conditions for activity. Here we, present the crystal structure of the protein complexed with NAD+ and, maltose, refined at a resolution of 1.9 A. The NAD+ is bound to a typical, Rossman fold NAD+-binding site, and the nicotinamide moiety is localized, close to the maltose substrate. Within the active site the conserved, Cys-174 and surrounding histidines are positioned to play a role in the, ... [(full description)]
About this Structure
1OBB is a [Single protein] structure of sequence from [Thermotoga maritima] with MAL and NAD as [ligands]. Active as [Alpha-glucosidase], with EC number [3.2.1.20]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:12588867
Page seeded by OCA on Tue Oct 30 11:11:51 2007
Categories: Alpha-glucosidase | Single protein | Thermotoga maritima | Hoffmann, V. | Liebl, W. | Lodge, J.A. | Maier, T. | Strater, N. | MAL | NAD | Glycosidase | Hydrolase | Maltose | Nad+ | Sulfinic acid
