1wp6

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[[Image:1wp6.jpg|left|200px]]
[[Image:1wp6.jpg|left|200px]]
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{{Structure
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|PDB= 1wp6 |SIZE=350|CAPTION= <scene name='initialview01'>1wp6</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1wp6", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltohexaosidase Glucan 1,4-alpha-maltohexaosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.98 3.2.1.98] </span>
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{{STRUCTURE_1wp6| PDB=1wp6 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp6 OCA], [http://www.ebi.ac.uk/pdbsum/1wp6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wp6 RCSB]</span>
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'''Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.'''
'''Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.'''
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[[Category: Kanai, R.]]
[[Category: Kanai, R.]]
[[Category: Yamane, K.]]
[[Category: Yamane, K.]]
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[[Category: alpha-amylase]]
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[[Category: Alpha-amylase]]
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[[Category: maltohexaose]]
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[[Category: Maltohexaose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:58:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:16 2008''
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Revision as of 10:58, 3 May 2008

Template:STRUCTURE 1wp6

Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.


Overview

Maltohexaose-producing amylase, called G6-amylase (EC 3.2.1.98), from alkalophilic Bacillus sp.707 predominantly produces maltohexaose (G6) from starch and related alpha-1,4-glucans. To elucidate the reaction mechanism of G6-amylase, the enzyme activities were evaluated and crystal structures were determined for the native enzyme and its complex with pseudo-maltononaose at 2.1 and 1.9 A resolutions, respectively. The optimal condition for starch-degrading reaction activity was found at 45 degrees C and pH 8.8, and the enzyme produced G6 in a yield of more than 30% of the total products from short-chain amylose (DP = 17). The crystal structures revealed that Asp236 is a nucleophilic catalyst and Glu266 is a proton donor/acceptor. Pseudo-maltononaose occupies subsites -6 to +3 and induces the conformational change of Glu266 and Asp333 to form a salt linkage with the N-glycosidic amino group and a hydrogen bond with secondary hydroxyl groups of the cyclitol residue bound to subsite -1, respectively. The indole moiety of Trp140 is stacked on the cyclitol and 4-amino-6-deoxyglucose residues located at subsites -6 and -5 within a 4 A distance. Such a face-to-face short contact may regulate the disposition of the glucosyl residue at subsite -6 and would govern the product specificity for G6 production.

About this Structure

1WP6 is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

Reference

Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Biochemistry. 2004 Nov 9;43(44):14047-56. PMID:15518553 Page seeded by OCA on Sat May 3 13:58:18 2008

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