2c45: Difference between revisions

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New page: left|200px<br /><applet load="2c45" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c45, resolution 2.99Å" /> '''NATIVE PRECURSOR OF ...
 
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[[Image:2c45.jpg|left|200px]]<br /><applet load="2c45" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2c45.jpg|left|200px]]<br /><applet load="2c45" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2c45, resolution 2.99&Aring;" />
caption="2c45, resolution 2.99&Aring;" />
'''NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE'''<br />
'''NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE'''<br />


==Overview==
==Overview==
L-aspartate-alpha-decarboxylase (ADC) is a critical regulatory enzyme in, the pantothenate biosynthetic pathway and belongs to a small class of, self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The, expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed, by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody, using whole cell lysate and immunoelectron microscopy. The recombinant ADC, proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E., coli and the protein structure was determined at 2.99 A resolution. The, proteins fold into the double-psi beta-barrel structure. The subunits of, the two tetramers (there are eight ADC molecules in the asymmetric unit), form pseudo fourfold rotational symmetry, similar to the E. coli ADC, proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is, of substantial interest for structure-based drug development.
L-aspartate-alpha-decarboxylase (ADC) is a critical regulatory enzyme in the pantothenate biosynthetic pathway and belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody using whole cell lysate and immunoelectron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 A resolution. The proteins fold into the double-psi beta-barrel structure. The subunits of the two tetramers (there are eight ADC molecules in the asymmetric unit) form pseudo fourfold rotational symmetry, similar to the E. coli ADC proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is of substantial interest for structure-based drug development.


==About this Structure==
==About this Structure==
2C45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C45 OCA].  
2C45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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=2C45 OCA].  


==Reference==
==Reference==
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[[Category: zymogen]]
[[Category: zymogen]]


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Revision as of 17:44, 21 February 2008

File:2c45.jpg


2c45, resolution 2.99Å

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NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

OverviewOverview

L-aspartate-alpha-decarboxylase (ADC) is a critical regulatory enzyme in the pantothenate biosynthetic pathway and belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody using whole cell lysate and immunoelectron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 A resolution. The proteins fold into the double-psi beta-barrel structure. The subunits of the two tetramers (there are eight ADC molecules in the asymmetric unit) form pseudo fourfold rotational symmetry, similar to the E. coli ADC proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is of substantial interest for structure-based drug development.

About this StructureAbout this Structure

2C45 is a Single protein structure of sequence from [1]. Active as Aspartate 1-decarboxylase, with EC number 4.1.1.11 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis., Gopalan G, Chopra S, Ranganathan A, Swaminathan K, Proteins. 2006 Dec 1;65(4):796-802. PMID:17001646

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