1ht6

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(New page: 200px<br /><applet load="1ht6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ht6, resolution 1.50&Aring;" /> '''CRYSTAL STRUCTURE AT...)
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[[Image:1ht6.jpg|left|200px]]<br /><applet load="1ht6" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1ht6, resolution 1.50&Aring;" />
'''CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1'''<br />
'''CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1'''<br />
==Overview==
==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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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==
==About this Structure==
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1HT6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with CA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HT6 OCA].
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1HT6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT6 OCA].
==Reference==
==Reference==
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[[Category: isozyme 1]]
[[Category: isozyme 1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:48:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:35 2008''

Revision as of 11:04, 21 February 2008

Image:1ht6.jpg

1ht6, resolution 1.50Å

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

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

1HT6 is a Single protein structure of sequence from Hordeum vulgare with and as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 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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