1ot1: Difference between revisions

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-[[Image:1ot1.jpg|left|200px]]
+{{Seed}}
+[[Image:1ot1.png|left|200px]]
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 {{STRUCTURE_1ot1|  PDB=1ot1  |  SCENE=  }}
-'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A'''
+===Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A===
-==Overview==
+<!--
-The alpha-amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141-157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen-bonded to Arg227, which does bind the substrate in the catalytic site. Using cyclodextrin glycosyltransferase as an example, this paper provides for the first time definite biochemical and structural evidence that Asp135 is required for the proper conformation of several catalytic site residues and therefore for activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_12706817}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12706817 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12706817}}
 ==About this Structure==
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 [[Category: Cyclodextrin]]
 [[Category: Glycosyl transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:15:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:09:30 2008''