1p6w

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[[Image:1p6w.jpg|left|200px]]<br /><applet load="1p6w" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1p6w.jpg|left|200px]]
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caption="1p6w, resolution 2.00&Aring;" />
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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)'''<br />
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{{Structure
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|PDB= 1p6w |SIZE=350|CAPTION= <scene name='initialview01'>1p6w</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE= AMY1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare])
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}}
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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==
==Overview==
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==About this Structure==
==About this Structure==
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1P6W 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=GLC:'>GLC</scene>, <scene name='pdbligand=SGC:'>SGC</scene>, <scene name='pdbligand=GTM:'>GTM</scene> and <scene name='pdbligand=CA:'>CA</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=1P6W OCA].
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1P6W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6W OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12906828 12906828]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12906828 12906828]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: x-ray diffraction]]
[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:43 2008''

Revision as of 11:20, 20 March 2008

Image:1p6w.jpg


PDB ID 1p6w

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , and
Gene: AMY1.1 (Hordeum vulgare)
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



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

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