1ot2

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{{STRUCTURE_1ot2| PDB=1ot2 | SCENE= }}
{{STRUCTURE_1ot2| PDB=1ot2 | SCENE= }}
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'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N'''
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===Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12706817 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12706817}}
==About this Structure==
==About this Structure==
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[[Category: Cyclodextrin]]
[[Category: Cyclodextrin]]
[[Category: Glycosyl transferase]]
[[Category: Glycosyl transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:03:05 2008''

Revision as of 06:03, 29 July 2008

Image:1ot2.png

Template:STRUCTURE 1ot2

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N

Template:ABSTRACT PUBMED 12706817

About this Structure

1OT2 is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity., Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L, FEBS Lett. 2003 Apr 24;541(1-3):47-51. PMID:12706817

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