1ot2: Difference between revisions

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New page: left|200px<br /><applet load="1ot2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ot2, resolution 2.10Å" /> '''Bacillus circulans s...
 
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[[Image:1ot2.jpg|left|200px]]<br /><applet load="1ot2" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ot2.jpg|left|200px]]<br /><applet load="1ot2" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ot2, resolution 2.10&Aring;" />
caption="1ot2, resolution 2.10&Aring;" />
'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N'''<br />
'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N'''<br />


==Overview==
==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 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.


==About this Structure==
==About this Structure==
1OT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with MAL, GLC, CA, EPE, MPD and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OT2 OCA].  
1OT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=EPE:'>EPE</scene>, <scene name='pdbligand=MPD:'>MPD</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT2 OCA].  


==Reference==
==Reference==
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[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dijkstra, B.W.]]
[[Category: Dijkstra, B W.]]
[[Category: Rozeboom, H.J.]]
[[Category: Rozeboom, H J.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: CA]]
[[Category: CA]]
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[[Category: glycosyl transferase]]
[[Category: glycosyl transferase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:14 2008''

Revision as of 15:21, 21 February 2008

File:1ot2.jpg


1ot2, resolution 2.10Å

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Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N

OverviewOverview

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.

About this StructureAbout this Structure

1OT2 is a Single protein structure of sequence from Bacillus circulans with , , , , and as ligands. Active as Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 Full crystallographic information is available from OCA.

ReferenceReference

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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