4cmr: Difference between revisions
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==The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04== | ==The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04== | ||
<StructureSection load='4cmr' size='340' side='right' caption='[[4cmr]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4cmr' size='340' side='right' caption='[[4cmr]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cmr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4cmr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_sp._st04 Pyrococcus sp. st04]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CMR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CMR FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4cmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmr OCA], [http://pdbe.org/4cmr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cmr RCSB], [http://www.ebi.ac.uk/pdbsum/4cmr 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=4cmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cmr OCA], [http://pdbe.org/4cmr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cmr RCSB], [http://www.ebi.ac.uk/pdbsum/4cmr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cmr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Pyrococcus sp. st04]] | |||
[[Category: Jung, J H]] | [[Category: Jung, J H]] | ||
[[Category: Park, C S]] | [[Category: Park, C S]] | ||
Revision as of 19:03, 16 November 2017
The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04The crystal structure of novel exo-type maltose-forming amylase(Py04_0872) from Pyrococcus sp. ST04
Structural highlights
Publication Abstract from PubMedA novel maltose-forming alpha-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows <13% amino-acid sequence identity to other known alpha-amylases and displays a unique enzymatic property in that it hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 A is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (beta/alpha)7-barrel fold and a C-domain (amino acids 342-597) composed of alpha-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is essential for specific cleavage of glucosidic bonds. The closed cavity at the active site is connected to a short substrate-binding channel that extends to the central hole of the tetramer, exhibiting a geometry that is significantly different from classical maltogenic amylases or beta-amylases. The structural features of this novel exo-type maltose-forming alpha-amylase provide a molecular basis for its unique enzymatic characteristics and for its potential use in industrial applications and protein engineering. Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04.,Park KH, Jung JH, Park SG, Lee ME, Holden JF, Park CS, Woo EJ Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1659-68. doi:, 10.1107/S1399004714006567. Epub 2014 May 30. PMID:24914977[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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