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1p6w
From Proteopedia
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'''Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)''' | '''Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)''' | ||
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[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: Robert, X.]] | [[Category: Robert, X.]] | ||
| - | [[Category: | + | [[Category: Alpha-amylase]] |
| - | [[Category: | + | [[Category: Barley]] |
| - | [[Category: | + | [[Category: Beta-alpha-barrel]] |
| - | [[Category: | + | [[Category: Isozyme 1]] |
| - | [[Category: | + | [[Category: Substrate analogue]] |
| - | [[Category: | + | [[Category: Sugar tongs binding site]] |
| - | [[Category: | + | [[Category: X-ray diffraction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:45:48 2008'' | |
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Revision as of 01:45, 3 May 2008
Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)
Overview
Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing maltooligosaccharides, not earlier reported for other alpha-amylases and probably associated with the different activity of AMY1 and AMY2 toward starch granules, has been identified. It is located in the C-terminal part of the enzyme and, thus, highlights a potential role of domain C. In order to scrutinize the possible biological significance of this domain in alpha-amylases, a thorough comparison of their three-dimensional structures was conducted. An additional role for an earlier-identified starch granule binding surface site is proposed, and a new calcium ion is reported.
About this Structure
1P6W is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
Reference
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs., Robert X, Haser R, Gottschalk TE, Ratajczak F, Driguez H, Svensson B, Aghajari N, Structure. 2003 Aug;11(8):973-84. PMID:12906828 Page seeded by OCA on Sat May 3 04:45:48 2008
