From Proteopedia
			(Difference between revisions)
												
			proteopedia linkproteopedia link
			
			
			
			
			
			
				|  |  | 
		| Line 1: | Line 1: | 
| - | [[Image:2b5d.gif|left|200px]] | + | {{Seed}} | 
|  | + | [[Image:2b5d.png|left|200px]] | 
|  |  |  |  | 
|  | <!-- |  | <!-- | 
| Line 9: | Line 10: | 
|  | {{STRUCTURE_2b5d|  PDB=2b5d  |  SCENE=  }}  |  | {{STRUCTURE_2b5d|  PDB=2b5d  |  SCENE=  }}  | 
|  |  |  |  | 
| - | '''Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima'''
 | + | ===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. Thecrystal 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 toa group of asyet 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 theTIM-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.
 | + | The line below this paragraph, {{ABSTRACT_PUBMED_16510973}}, adds the Publication Abstract to the page  | 
|  | + | (as it appears on PubMed at http://www.pubmed.gov), where 16510973 is the PubMed ID number. | 
|  | + | --> | 
|  | + | {{ABSTRACT_PUBMED_16510973}} | 
|  |  |  |  | 
|  | ==About this Structure== |  | ==About this Structure== | 
| Line 25: | Line 29: | 
|  | [[Category: Ficner, R.]] |  | [[Category: Ficner, R.]] | 
|  | [[Category: Liebl, W.]] |  | [[Category: Liebl, W.]] | 
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:52:38 2008'' | + |   | 
|  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:47:55 2008'' | 
Revision as of 06:47, 29 July 2008
Template:STRUCTURE 2b5d 
 Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritima
Template:ABSTRACT PUBMED 16510973
 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 Tue Jul 29 09:47:55 2008