1pyd: Difference between revisions

Revision as of 04:10, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pyd.png

Template:STRUCTURE 1pyd

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

Template:ABSTRACT PUBMED 8512926

About this StructureAbout this Structure

1PYD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution., Dyda F, Furey W, Swaminathan S, Sax M, Farrenkopf B, Jordan F, Biochemistry. 1993 Jun 22;32(24):6165-70. PMID:8512926

Page seeded by OCA on Mon Jul 28 04:10:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1pyd.jpg|left|200px]]
+{{Seed}}
+[[Image:1pyd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{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''