Alcohol dehydrogenase from Clostridium beijerinckii

[[Image:2b831.png|left|200px]]

[[Image:2b831.png|left|200px]]

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{{STRUCTURE_2b83| PDB=2b83 | SCENE=2b83/Tetramer/1 }}

{{STRUCTURE_2b83| PDB=2b83 | SCENE=2b83/Tetramer/1 }}

===A single amino acid substitution in the ''Clostridium beijerinckii'' alcohol dehydrogenase is critical for thermostabilization===

===A single amino acid substitution in the ''Clostridium beijerinckii'' alcohol dehydrogenase is critical for thermostabilization===

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{{ABSTRACT_PUBMED_17063493}}

{{ABSTRACT_PUBMED_17063493}}

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The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of [http://en.wikipedia.org/wiki/Clostridium_beijerinckii ''Clostridium beijerinckii''] [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase alcohol dehydrogenase] (CbADH; [http://www.expasy.org/enzyme/1.1.1.2 EC 1.1.1.2]) with the [http://en.wikipedia.org/wiki/Mutation substitution] Q100P (<scene name='2b83/Tet/3'>tetramer</scene>) was solved at 2.25 Å resolution. The <scene name='2b83/Mut/1'>substitution</scene> of Gln100 with Pro did not cause significant structural changes in the protein structure. The residues of the <font color='lime'><b>wildtype protein are colored lime</b></font> and the residues of the <font color='cyan'><b>mutant one in cyan</b></font>. Only [http://en.wikipedia.org/wiki/Hydrogen_bond 2 H-bonds] were lost, one between Oε1 of Gln100 and the main chain N of Gly297, and the second between Nε2 of Gln100 and the main chain carbonyl O of Gly297. The mutation caused that an additional CH₂ group (Cδ of Pro100) is surrounded by nonpolar residues: Pro88 (3.8 Å), Trp90 (3.5 Å), and Val95 (4 Å). These residues (P100, P88, W90, and V95) are situated on a protruding lobe of the protein. An additional 11 [http://en.wikipedia.org/wiki/Aliphatic_compound aliphatic] and [http://en.wikipedia.org/wiki/Aromatic aromatic] carbon atoms are situated within the distance of 6 Å from Cδ of Pro100 (two [http://en.wikipedia.org/wiki/Methyl_group methyl groups] of Val95; three carbon atoms of the Trp90 [http://en.wikipedia.org/wiki/Indole indole] group; Cβ and Cγ [http://en.wikipedia.org/wiki/Methylene methylene] groups of Pro100; Cβ and Cγ of Gln101, and two carbons of the Phe99 [http://en.wikipedia.org/wiki/Phenyl_group phenyl] ring).

The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of [http://en.wikipedia.org/wiki/Clostridium_beijerinckii ''Clostridium beijerinckii''] [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase alcohol dehydrogenase] (CbADH; [http://www.expasy.org/enzyme/1.1.1.2 EC 1.1.1.2]) with the [http://en.wikipedia.org/wiki/Mutation substitution] Q100P (<scene name='2b83/Tet/3'>tetramer</scene>) was solved at 2.25 Å resolution. The <scene name='2b83/Mut/1'>substitution</scene> of Gln100 with Pro did not cause significant structural changes in the protein structure. The residues of the <font color='lime'><b>wildtype protein are colored lime</b></font> and the residues of the <font color='cyan'><b>mutant one in cyan</b></font>. Only [http://en.wikipedia.org/wiki/Hydrogen_bond 2 H-bonds] were lost, one between Oε1 of Gln100 and the main chain N of Gly297, and the second between Nε2 of Gln100 and the main chain carbonyl O of Gly297. The mutation caused that an additional CH₂ group (Cδ of Pro100) is surrounded by nonpolar residues: Pro88 (3.8 Å), Trp90 (3.5 Å), and Val95 (4 Å). These residues (P100, P88, W90, and V95) are situated on a protruding lobe of the protein. An additional 11 [http://en.wikipedia.org/wiki/Aliphatic_compound aliphatic] and [http://en.wikipedia.org/wiki/Aromatic aromatic] carbon atoms are situated within the distance of 6 Å from Cδ of Pro100 (two [http://en.wikipedia.org/wiki/Methyl_group methyl groups] of Val95; three carbon atoms of the Trp90 [http://en.wikipedia.org/wiki/Indole indole] group; Cβ and Cγ [http://en.wikipedia.org/wiki/Methylene methylene] groups of Pro100; Cβ and Cγ of Gln101, and two carbons of the Phe99 [http://en.wikipedia.org/wiki/Phenyl_group phenyl] ring).

==About this Structure==

==About this Structure==

2B83 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B83 OCA].

2B83 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B83 OCA].

==Reference==

==Reference==