1zpd
From Proteopedia
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'''PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS''' | '''PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS''' | ||
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[[Category: Lu, G.]] | [[Category: Lu, G.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: | + | [[Category: Alcohol fermentation]] |
| - | [[Category: | + | [[Category: Decarboxylase]] |
| - | [[Category: | + | [[Category: Thiamin diphosphate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:54:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:54, 3 May 2008
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| 1zpd, resolution 1.86Å () | |||||||||
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| Ligands: | , , | ||||||||
| Activity: | Pyruvate decarboxylase, with EC number 4.1.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS
Overview
The crystal structure of tetrameric pyruvate decarboxylase from Zymomonas mobilis has been determined at 1.9 A resolution and refined to a crystallographic R-factor of 16.2% and Rfree of 19.7%. The subunit consists of three domains, all of the alpha/beta type. Two of the subunits form a tight dimer with an extensive interface area. The thiamin diphosphate binding site is located at the subunit-subunit interface, and the cofactor, bound in the V conformation, interacts with residues from the N-terminal domain of one subunit and the C-terminal domain of the second subunit. The 2-fold symmetry generates the second thiamin diphosphate binding site in the dimer. Two of the dimers form a tightly packed tetramer with pseudo 222 symmetry. The interface area between the dimers is much larger in pyruvate decarboxylase from Z. mobilis than in the yeast enzyme, and structural differences in these parts result in a completely different packing of the subunits in the two enzymes. In contrast to other pyruvate decarboxylases, the enzyme from Z. mobilis is not subject to allosteric activation by the substrate. The tight packing of the dimers in the tetramer prevents large rearrangements in the quaternary structure as seen in the yeast enzyme and locks the enzyme in an activated conformation. The architecture of the cofactor binding site and the active site is similar in the two enzymes. However, the x-ray analysis reveals subtle but significant structural differences in the active site that might be responsible for variations in the biochemical properties in these enzymes.
About this Structure
1ZPD is a Single protein structure of sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.
Reference
High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases., Dobritzsch D, Konig S, Schneider G, Lu G, J Biol Chem. 1998 Aug 7;273(32):20196-204. PMID:9685367 Page seeded by OCA on Sat May 3 17:54:36 2008
