1uhd
From Proteopedia
(New page: 200px<br /><applet load="1uhd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uhd, resolution 2.00Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1uhd.jpg|left|200px]]<br /><applet load="1uhd" size=" | + | [[Image:1uhd.jpg|left|200px]]<br /><applet load="1uhd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uhd, resolution 2.00Å" /> | caption="1uhd, resolution 2.00Å" /> | ||
'''Crystal structure of aspartate decarboxylase, pyruvoly group bound form'''<br /> | '''Crystal structure of aspartate decarboxylase, pyruvoly group bound form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | l-Aspartate alpha-decarboxylase (ADC), encoded by the panD gene, catalyzes | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1UHD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] Full crystallographic information is available from [http:// | + | 1UHD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHD OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Han, B | + | [[Category: Han, B W.]] |
| - | [[Category: Kwon, A | + | [[Category: Kwon, A R.]] |
| - | [[Category: Lee, B | + | [[Category: Lee, B I.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: double-psi beta barrel]] | [[Category: double-psi beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:33 2008'' |
Revision as of 13:24, 21 February 2008
|
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.
About this Structure
1UHD is a Protein complex structure of sequences from Helicobacter pylori. Active as Aspartate 1-decarboxylase, with EC number 4.1.1.11 Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 15:24:33 2008
