2b5d
From Proteopedia
(Difference between revisions)
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<StructureSection load='2b5d' size='340' side='right'caption='[[2b5d]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2b5d' size='340' side='right'caption='[[2b5d]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2b5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2b5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5D FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
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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=2b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5d OCA], [https://pdbe.org/2b5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5d RCSB], [https://www.ebi.ac.uk/pdbsum/2b5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5d ProSAT]</span></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=2b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5d OCA], [https://pdbe.org/2b5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5d RCSB], [https://www.ebi.ac.uk/pdbsum/2b5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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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=2b5d ConSurf]. | </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=2b5d ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | alpha-Amylases are essential enzymes in alpha-glucan metabolism and catalyse the hydrolysis of long sugar polymers such as amylose and starch. The crystal structure of a previously unidentified amylase (AmyC) from the hyperthermophilic organism Thermotoga maritima was determined at 2.2 Angstroms resolution by means of MAD. AmyC lacks sequence similarity to canonical alpha-amylases, which belong to glycosyl hydrolase families 13, 70 and 77, but exhibits significant similarity to a group of as yet uncharacterized proteins in COG1543 and is related to glycerol hydrolase family 57 (GH-57). AmyC reveals features that are characteristic of alpha-amylases, such as a distorted TIM-barrel structure formed by seven beta-strands and alpha-helices (domain A), and two additional but less well conserved domains. The latter are domain B, which contains three helices inserted in the TIM-barrel after beta-sheet 2, and domain C, a five-helix region at the C-terminus. Interestingly, despite moderate sequence homology, structure comparison revealed significant similarities to a member of GH-57 with known three-dimensional structure, Thermococcus litoralis 4-glucanotransferase, and an even higher similarity to a structure of an enzyme of unknown function from Thermus thermophilus. | ||
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| - | Structure of the novel alpha-amylase AmyC from Thermotoga maritima.,Dickmanns A, Ballschmiter M, Liebl W, Ficner R Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):262-70. Epub 2006, Feb 22. PMID:16510973<ref>PMID:16510973</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2b5d" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Amylase 3D structures|Amylase 3D structures]] | *[[Amylase 3D structures|Amylase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Alpha-amylase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Ballschmiter | + | [[Category: Ballschmiter M]] |
| - | [[Category: Dickmanns | + | [[Category: Dickmanns A]] |
| - | [[Category: Ficner | + | [[Category: Ficner R]] |
| - | [[Category: Liebl | + | [[Category: Liebl W]] |
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Current revision
Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima
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