1p6w

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[[Image:1p6w.jpg|left|200px]]
 
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{{Structure
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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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|PDB= 1p6w |SIZE=350|CAPTION= <scene name='initialview01'>1p6w</scene>, resolution 2.00&Aring;
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<StructureSection load='1p6w' size='340' side='right'caption='[[1p6w]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>
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<table><tr><td colspan='2'>[[1p6w]] 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=1P6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6W FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6w OCA], [https://pdbe.org/1p6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6w RCSB], [https://www.ebi.ac.uk/pdbsum/1p6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6w ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ht6|1HT6]], [[1amy|1AMY]], [[1bg9|1BG9]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6w OCA], [http://www.ebi.ac.uk/pdbsum/1p6w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p6w RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMY1_HORVU AMY1_HORVU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p6/1p6w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p6w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''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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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<ref>PMID:12906828</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1p6w" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==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://www.ncbi.nlm.nih.gov/pubmed/12906828 12906828]
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[[Category: Alpha-amylase]]
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aghajari, N.]]
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[[Category: Aghajari N]]
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[[Category: Haser, R.]]
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[[Category: Haser R]]
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[[Category: Robert, X.]]
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[[Category: Robert X]]
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[[Category: alpha-amylase]]
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[[Category: barley]]
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[[Category: beta-alpha-barrel]]
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[[Category: isozyme 1]]
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[[Category: substrate analogue]]
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[[Category: sugar tongs binding site]]
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[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:55:42 2008''
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Current revision

Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)

PDB ID 1p6w

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