2uyb
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2uyb.gif|left|200px]] | [[Image:2uyb.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2uyb", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2uyb| PDB=2uyb | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''S161A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC''' | '''S161A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC''' | ||
| Line 33: | Line 30: | ||
[[Category: Mcrobbie, I.]] | [[Category: Mcrobbie, I.]] | ||
[[Category: Stevenson, C E.M.]] | [[Category: Stevenson, C E.M.]] | ||
| - | [[Category: | + | [[Category: Cupin]] |
| - | [[Category: | + | [[Category: Decarboxylase]] |
| - | [[Category: | + | [[Category: Formate]] |
| - | [[Category: | + | [[Category: Lyase]] |
| - | [[Category: | + | [[Category: Manganese]] |
| - | [[Category: | + | [[Category: Metal binding protein]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Oxalate]] |
| - | [[Category: | + | [[Category: S161a mutant]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:48:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:48, 4 May 2008
S161A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC
Overview
Oxalate decarboxylase (EC 4.1.1.2) catalyses the conversion of oxalate into carbon dioxide and formate. It requires manganese and, uniquely, dioxygen for catalysis. It forms a homohexamer and each subunit contains two similar, but distinct, manganese sites termed sites 1 and 2. There is kinetic evidence that only site 1 is catalytically active and that site 2 is purely structural. However, the kinetics of enzymes with mutations in site 2 are often ambiguous and all mutant kinetics have been interpreted without structural information. Nine new site-directed mutants have been generated and four mutant crystal structures have now been solved. Most mutants targeted (i) the flexibility (T165P), (ii) favoured conformation (S161A, S164A, D297A or H299A) or (iii) presence (Delta162-163 or Delta162-164) of a lid associated with site 1. The kinetics of these mutants were consistent with only site 1 being catalytically active. This was particularly striking with D297A and H299A because they disrupted hydrogen bonds between the lid and a neighbouring subunit only when in the open conformation and were distant from site 2. These observations also provided the first evidence that the flexibility and stability of lid conformations are important in catalysis. The deletion of the lid to mimic the plant oxalate oxidase led to a loss of decarboxylase activity, but only a slight elevation in the oxalate oxidase side reaction, implying other changes are required to afford a reaction specificity switch. The four mutant crystal structures (R92A, E162A, Delta162-163 and S161A) strongly support the hypothesis that site 2 is purely structural.
About this Structure
2UYB is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations., Just VJ, Burrell MR, Bowater L, McRobbie I, Stevenson CE, Lawson DM, Bornemann S, Biochem J. 2007 Nov 1;407(3):397-406. PMID:17680775 Page seeded by OCA on Sun May 4 17:48:31 2008
