1qpr
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1qpr.gif|left|200px]] | [[Image:1qpr.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1qpr", 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_1qpr| PDB=1qpr | SCENE= }} | |
- | | | + | |
- | | | + | |
- | }} | + | |
'''QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP''' | '''QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP''' | ||
Line 24: | Line 21: | ||
Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target., Sharma V, Grubmeyer C, Sacchettini JC, Structure. 1998 Dec 15;6(12):1587-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9862811 9862811] | Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target., Sharma V, Grubmeyer C, Sacchettini JC, Structure. 1998 Dec 15;6(12):1587-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9862811 9862811] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
- | [[Category: Nicotinate-nucleotide diphosphorylase (carboxylating)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Grubmeyer, C.]] | [[Category: Grubmeyer, C.]] | ||
Line 30: | Line 26: | ||
[[Category: Sharma, V.]] | [[Category: Sharma, V.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
- | [[Category: | + | [[Category: De novo nad biosynthesis]] |
- | [[Category: | + | [[Category: Phosphoribosyltransferase]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Prpp]] |
- | [[Category: | + | [[Category: Prtase]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Quinolinic acid]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Tb structural genomics consortium]] |
- | [[Category: | + | [[Category: Tbsgc]] |
- | [[Category: | + | [[Category: Transferase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:33:47 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 03:33, 3 May 2008
QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP
Overview
Background:. Mycobacterium tuberculosis is the single most deadly human pathogen and is responsible for nearly three million deaths every year. Recent elucidation of the mode of action of isoniazid, a frontline antimycobacterial drug, suggests that NAD metabolism is extremely critical for this microorganism. M. tuberculosis depends solely on the de novo pathway to meet its NAD demand. Quinolinic acid phosphoribosyltransferase (QAPRTase), a key enzyme in the de novo biosynthesis of NAD, provides an attractive target for designing novel antitubercular drugs. Results:. The X-ray crystal structure of the M. tuberculosis QAPRTase apoenzyme has been determined by multiple isomorphous replacement at 2.4 A resolution. Structures of the enzyme have also been solved in complex with the substrate quinolinic acid (QA), the inhibitory QA analog phthalic acid (PA), the product nicotinate mononucleotide (NAMN), and as a ternary complex with PA and a substrate analog, 5-phosphoribosyl-1-(beta-methylene)pyrophosphate (PRPCP). The structure of the nonproductive QAPRTase-PA-PRPCP Michaelis complex reveals a 5-phosphoribosyl-1-pyrophosphate-binding site that is different from the one observed in type I phosphoribosyltransferases (PRTases). The type II PRTase active site of QAPRTase undergoes conformational changes that appear to be important in determining substrate specificity and eliciting productive catalysis. Conclusions:. QAPRTase is the only known representative of the type II PRTase fold, an unusual alpha/beta barrel, and appears to represent convergent evolution for PRTase catalysis. The active site of type II PRTase bears little resemblance to the better known type I enzymes.
About this Structure
1QPR is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target., Sharma V, Grubmeyer C, Sacchettini JC, Structure. 1998 Dec 15;6(12):1587-99. PMID:9862811 Page seeded by OCA on Sat May 3 06:33:47 2008
Categories: Mycobacterium tuberculosis | Single protein | Grubmeyer, C. | Sacchettini, J C. | Sharma, V. | TBSGC, TB Structural Genomics Consortium. | De novo nad biosynthesis | Phosphoribosyltransferase | Protein structure initiative | Prpp | Prtase | Psi | Quinolinic acid | Structural genomic | Tb structural genomics consortium | Tbsgc | Transferase