1p6w

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{{STRUCTURE_1p6w| PDB=1p6w | SCENE= }}
{{STRUCTURE_1p6w| PDB=1p6w | SCENE= }}
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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)'''
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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)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12906828 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12906828}}
==About this Structure==
==About this Structure==
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[[Category: Sugar tongs binding site]]
[[Category: Sugar tongs binding site]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:45:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:59:13 2008''

Revision as of 12:59, 27 July 2008

Image:1p6w.png

Template:STRUCTURE 1p6w

Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)

Template:ABSTRACT PUBMED 12906828

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

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