1zpd: Difference between revisions
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[[Image:1zpd.gif|left|200px]] | [[Image:1zpd.gif|left|200px]] | ||
'''PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS''' | {{Structure | ||
|PDB= 1zpd |SIZE=350|CAPTION= <scene name='initialview01'>1zpd</scene>, resolution 1.86Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=DPX:MONO-{4-[(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-AMINO]-2-HYDROXY-3-MERCAPTO-PENT-3-ENYL-PHOSPHONO}+ESTER'>DPX</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] | |||
|GENE= | |||
}} | |||
'''PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZPD is a [ | 1ZPD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9685367 9685367] | ||
[[Category: Pyruvate decarboxylase]] | [[Category: Pyruvate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thiamin diphosphate]] | [[Category: thiamin diphosphate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:38:16 2008'' | ||
Revision as of 16:38, 20 March 2008
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| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Pyruvate decarboxylase, with EC number 4.1.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS
OverviewOverview
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 StructureAbout this Structure
1ZPD is a Single protein structure of sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.
ReferenceReference
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
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