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2b5d
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(New page: 200px<br /><applet load="2b5d" size="350" color="white" frame="true" align="right" spinBox="true" caption="2b5d, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 16:17, 29 January 2008
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Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima
Overview
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.
About this Structure
2B5D is a Protein complex structure of sequences from Thermotoga maritima. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
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
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