1ji1: Difference between revisions
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==Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1== | ==Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1== | ||
<StructureSection load='1ji1' size='340' side='right' caption='[[1ji1]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1ji1' size='340' side='right' caption='[[1ji1]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ji2|1ji2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ji2|1ji2]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji1 OCA], [http://pdbe.org/1ji1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ji1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ji1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji1 OCA], [http://pdbe.org/1ji1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ji1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ji1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ji1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1ji1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1ji1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1ji1" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1ji1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:19, 17 January 2018
Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1
Structural highlights
Function[NEPU1_THEVU] Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Also hydrolyzes cyclodextrins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe X-ray crystal structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) and alpha-amylase 2 (TVAII) have been determined at 1.6 A and 2.3 A resolution, respectively. The structures of TVAI and TVAII have been refined, R-factor of 0.182 (R(free)=0.206) and 0.179 (0.224), respectively, with good chemical geometries. Both TVAI and TVAII have four domains, N, A, B and C, and all very similar in structure. However, there are some differences in the structures between them. Domain N of TVAI interacts strongly with domains A and B, giving a spherical shape structure to the enzyme, while domain N of TVAII is isolated from the other domains, which leads to the formation of a dimer. TVAI has three bound Ca ions, whereas TVAII has only one. TVAI has eight extra loops compared to TVAII, while TVAII has two extra loops compared to TVAI. TVAI can hydrolyze substrates more efficiently than TVAII with a high molecular mass such as starch, while TVAII is much more active against cyclodextrins than TVAI and other alpha-amylases. A structural comparison of the active sites has clearly revealed this difference in substrate specificity. Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution.,Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y J Mol Biol. 2002 Apr 26;318(2):443-53. PMID:12051850[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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