1MZV

Crystal Structure of Adenine Phosphoribosyltransferase (APRT) From Leishmania tarentolae

Summary for 1MZV

• Entry DOI: 10.2210/pdb1mzv/pdb
• Related: 1qb7
• Descriptor: Adenine Phosphoribosyltransferase, PHOSPHATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: alpha/beta structure, transferase
• Biological source: Leishmania tarentolae
• Total number of polymer chains: 1
• Total formula weight: 26356.02

Authors

Thiemann, O.H.,Silva, M.,Oliva, G.,Silva, C.H.T.P.,Iulek, J. (deposition date: 2002-10-10, release date: 2003-10-28, Last modification date: 2024-02-14)

Primary citation

Silva, M.,Silva, C.H.T.P.,Iulek, J.,Oliva, G.,Thiemann, O.H.
Crystal structure of adenine phosphoribosyltransferase from Leishmania tarentolae: potential implications for APRT catalytic mechanism.
Biochim.Biophys.Acta, 1696:31-39, 2004

PubMed Abstract: The three-dimensional structure of Leishmania tarentolae adenine phosphoribosyltransferase (APRT) in complex with adenosine-5-monophosphate (AMP) and a phosphate ion has been solved. Refinement against X-ray diffraction data extending to 2.2-A resolution led to a final crystallographic R factor of 18.3%. Structural comparisons amongst this APRT enzyme and other 'type I' PRTases whose structures have been determined reveal several important features of the PRTases catalytic mechanism. Based on structural superpositions and molecular interaction potential calculations, it was possible to suggest that the PRPP is the first substrate to bind, while the AMP is the last product to leave the active site, in accordance to recent kinetic studies performed with the Leishmania donovani APRT.

PubMed: 14726202
DOI: 10.1016/j.bbapap.2003.09.003

Experimental method

X-RAY DIFFRACTION (2.2 Å)