1uhd: Difference between revisions

Revision as of 08:10, 29 July 2008

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File:1uhd.png

Template:STRUCTURE 1uhd

Crystal structure of aspartate decarboxylase, pyruvoly group bound formCrystal structure of aspartate decarboxylase, pyruvoly group bound form

Template:ABSTRACT PUBMED 15184017

About this StructureAbout this Structure

1UHD is a Protein complex structure of sequences from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase., Lee BI, Suh SW, J Mol Biol. 2004 Jun 25;340(1):1-7. PMID:15184017

Page seeded by OCA on Tue Jul 29 08:10:50 2008

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OCA

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-[[Image:1uhd.jpg|left|200px]]
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-'''Crystal structure of aspartate decarboxylase, pyruvoly group bound form'''
+===Crystal structure of aspartate decarboxylase, pyruvoly group bound form===
-==Overview==
+<!--
-l-Aspartate alpha-decarboxylase (ADC), encoded by the panD gene, catalyzes the conversion of l-aspartate into beta-alanine. In the microorganisms, beta-alanine is required for the synthesis of pantothenate (vitamin B(5)), which is the precursor of 4'-phosphopantetheine and coenzyme A. We have determined the crystal structure of Helicobacter pylori ADC, a tetrameric enzyme, in two forms: the apo structure at 2.0 A resolution and the isoasparagine complex structure at 1.55 A resolution. All subunits of the tetramer are self-processed at the Gly24-Ser25 linkage, producing the smaller beta chain (residues 1-24) and the larger alpha chain (residues 25-117). Each subunit contains nine beta-strands and three alpha-helices; it is folded into the double-psi beta-barrel structure. In the apo structure, the new amino terminus of the alpha chain, Ser25, is converted into a pyruvoyl group. In the isoasparagine complex structure, the substrate analog is covalently attached to the pyruvoyl group. This structure represents the enzyme-substrate Schiff base intermediate that was proposed to form prior to the decarboxylation step in the catalytic cycle of ADC. Thus our study provides direct structural evidence for the reaction mechanism of ADC.
+The line below this paragraph, {{ABSTRACT_PUBMED_15184017}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15184017 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15184017}}
 ==About this Structure==
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 [[Category: Suh, S W.]]
 [[Category: Double-psi beta barrel]]
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