1QPR

QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP

Summary for 1QPR

• Entry DOI: 10.2210/pdb1qpr/pdb
• Descriptor: QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE, MANGANESE (II) ION, PHTHALIC ACID, ... (5 entities in total)
• Functional Keywords: prtase, de novo nad biosynthesis, prpp, transferase, phosphoribosyltransferase, quinolinic acid, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 6
• Total formula weight: 183089.80

Authors

Sharma, V.,Grubmeyer, C.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 1998-10-17, release date: 1998-10-21, Last modification date: 2024-02-14)

Primary citation

Sharma, V.,Grubmeyer, C.,Sacchettini, J.C.
Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.
Structure, 6:1587-1599, 1998

PubMed Abstract: . 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.

PubMed: 9862811
DOI: 10.1016/S0969-2126(98)00156-7

Experimental method

X-RAY DIFFRACTION (2.45 Å)