1ht6: Difference between revisions

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[[Image:1ht6.jpg|left|200px]]
[[Image:1ht6.jpg|left|200px]]


{{Structure
<!--
|PDB= 1ht6 |SIZE=350|CAPTION= <scene name='initialview01'>1ht6</scene>, resolution 1.50&Aring;
The line below this paragraph, containing "STRUCTURE_1ht6", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1ht6| PDB=1ht6  | SCENE= }}  
|RELATEDENTRY=[[1amy|1AMY]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht6 OCA], [http://www.ebi.ac.uk/pdbsum/1ht6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ht6 RCSB]</span>
}}


'''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'''
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[[Category: Haser, R.]]
[[Category: Haser, R.]]
[[Category: Robert, X.]]
[[Category: Robert, X.]]
[[Category: alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: barley]]
[[Category: Barley]]
[[Category: beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]
[[Category: isozyme 1]]
[[Category: Isozyme 1]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:12:22 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:04 2008''

Revision as of 16:12, 2 May 2008

File:1ht6.jpg

Template:STRUCTURE 1ht6

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. 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 Fri May 2 19:12:22 2008

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