1ht6: Difference between revisions

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New page: left|200px<br /><applet load="1ht6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ht6, resolution 1.50Å" /> '''CRYSTAL STRUCTURE AT...
 
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[[Image:1ht6.jpg|left|200px]]<br /><applet load="1ht6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ht6, resolution 1.50&Aring;" />
'''CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1'''<br />


==Overview==
==CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1==
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.
<StructureSection load='1ht6' size='340' side='right'caption='[[1ht6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ht6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HT6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht6 OCA], [https://pdbe.org/1ht6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ht6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ht6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ht6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMY1_HORVU AMY1_HORVU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1ht6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ht6 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Amylase 3D structures|Amylase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Alpha-amylase]]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aghajari, N.]]
[[Category: Aghajari N]]
[[Category: Haser, R.]]
[[Category: Haser R]]
[[Category: Robert, X.]]
[[Category: Robert X]]
[[Category: CA]]
[[Category: EDO]]
[[Category: alpha-amylase]]
[[Category: barley]]
[[Category: beta-alpha-barrel]]
[[Category: isozyme 1]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:48:50 2007''

Latest revision as of 07:30, 7 February 2024

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

1ht6, resolution 1.50Å

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