2c45
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2c45.jpg|left|200px]] | [[Image:2c45.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2c45", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_2c45| PDB=2c45 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE''' | '''NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE''' | ||
Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 2C45 is a [[Single protein]] structure | + | 2C45 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C45 OCA]. |
==Reference== | ==Reference== | ||
Line 29: | Line 26: | ||
[[Category: Ranganathan, A.]] | [[Category: Ranganathan, A.]] | ||
[[Category: Swaminathan, K.]] | [[Category: Swaminathan, K.]] | ||
- | [[Category: | + | [[Category: Carboxylase]] |
- | [[Category: | + | [[Category: Decarboxylase]] |
- | [[Category: | + | [[Category: Double-psi beta barrel]] |
- | [[Category: | + | [[Category: Lyase]] |
- | [[Category: | + | [[Category: Pantothenate biosynthesis]] |
- | [[Category: | + | [[Category: Pyruvate]] |
- | [[Category: | + | [[Category: Zymogen]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:13:22 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 18:13, 3 May 2008
NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
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.
About this Structure
2C45 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 21:13:22 2008