1ht6: Difference between revisions

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[[Image:1ht6.jpg|left|200px]]
{{Seed}}
[[Image:1ht6.png|left|200px]]


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{{STRUCTURE_1ht6|  PDB=1ht6  |  SCENE=  }}  
{{STRUCTURE_1ht6|  PDB=1ht6  |  SCENE=  }}  


'''CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1'''
===CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_12906828}}, adds the Publication Abstract to the page
(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: Beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]
[[Category: Isozyme 1]]
[[Category: Isozyme 1]]
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