2b5d
From Proteopedia
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'''Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima''' | '''Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/16510973 16510973] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16510973 16510973] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Thermotoga maritima]] | ||
[[Category: Ballschmiter, M.]] | [[Category: Ballschmiter, M.]] | ||
[[Category: Dickmanns, A.]] | [[Category: Dickmanns, A.]] | ||
[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
[[Category: Liebl, W.]] | [[Category: Liebl, W.]] | ||
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Revision as of 16:52, 3 May 2008
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
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 Page seeded by OCA on Sat May 3 19:52:38 2008
