1pyd: Difference between revisions

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[[Image:1pyd.~~jpg~~|left|200px]]

[[Image:1pyd.png|left|200px]]

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~~'''~~CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION~~'''~~

===CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION===

~~==Overview==~~

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~~The crystal structure of brewers' yeast pyruvate decarboxylase, a thiamin diphosphate dependent alpha~~-~~keto acid decarboxylase, has been determined to 2.4~~-~~A resolution.~~ The ~~homotetrameric assembly contains two dimers~~, ~~exhibiting strong intermonomer interactions within each dimer but more limited ones between dimers. Each monomeric subunit is partitioned into three structural domains~~, ~~all folding according~~ to ~~a mixed alpha~~/~~beta motif~~. ~~Two of these domains are associated with cofactor binding~~, ~~while the other~~ is ~~associated with substrate activation. The catalytic centers containing both thiamin diphosphate and Mg(II) are located deep in~~ the ~~intermonomer interface within each dimer. Amino acids important in cofactor binding and likely to participate in catalysis and substrate activation are identified~~.

The line below this paragraph, {{ABSTRACT_PUBMED_8512926}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8512926 is the PubMed ID number.

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==About this Structure==

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[[Category: Dyda, F.]]

[[Category: Furey, W.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 05~~:38:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:10:41 2008''

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-[[Image:1pyd.jpg|left|200px]]
+{{Seed}}
+[[Image:1pyd.png|left|200px]]
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 {{STRUCTURE_1pyd|  PDB=1pyd  |  SCENE=  }}
-'''CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION'''
+===CATALYTIC CENTERS IN THE THIAMIN DIPHOSPHATE DEPENDENT ENZYME PYRUVATE DECARBOXYLASE AT 2.4 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structure of brewers' yeast pyruvate decarboxylase, a thiamin diphosphate dependent alpha-keto acid decarboxylase, has been determined to 2.4-A resolution. The homotetrameric assembly contains two dimers, exhibiting strong intermonomer interactions within each dimer but more limited ones between dimers. Each monomeric subunit is partitioned into three structural domains, all folding according to a mixed alpha/beta motif. Two of these domains are associated with cofactor binding, while the other is associated with substrate activation. The catalytic centers containing both thiamin diphosphate and Mg(II) are located deep in the intermonomer interface within each dimer. Amino acids important in cofactor binding and likely to participate in catalysis and substrate activation are identified.
+The line below this paragraph, {{ABSTRACT_PUBMED_8512926}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8512926 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8512926}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Dyda, F.]]
 [[Category: Furey, W.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:38:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:10:41 2008''