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Crystal structure of Sus scrofa quinolinate phosphoribosyltransferase in complex with nicotinate mononucleotide.
PLoS One. 2013; 8(4):e62027.Plos

Abstract

We have determined the crystal structure of porcine quinolinate phosphoribosyltransferase (QAPRTase) in complex with nicotinate mononucleotide (NAMN), which is the first crystal structure of a mammalian QAPRTase with its reaction product. The structure was determined from protein obtained from the porcine kidney. Because the full protein sequence of porcine QAPRTase was not available in either protein or nucleotide databases, cDNA was synthesized using reverse transcriptase-polymerase chain reaction to determine the porcine QAPRTase amino acid sequence. The crystal structure revealed that porcine QAPRTases have a hexameric structure that is similar to other eukaryotic QAPRTases, such as the human and yeast enzymes. However, the interaction between NAMN and porcine QAPRTase was different from the interaction found in prokaryotic enzymes, such as those of Helicobacter pylori and Mycobacterium tuberculosis. The crystal structure of porcine QAPRTase in complex with NAMN provides a structural framework for understanding the unique properties of the mammalian QAPRTase active site and designing new antibiotics that are selective for the QAPRTases of pathogenic bacteria, such as H. pylori and M. tuberculosis.

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Authors+Show Affiliations

Youn HS
School of Life Sciences, Gwangju Institute of Science & Technology, Gwangju, Republic of Korea.
Kim MK
No affiliation info available
Kang GB
No affiliation info available
Kim TG
No affiliation info available
Lee JG
No affiliation info available
An JY
No affiliation info available
Park KR
No affiliation info available
Lee Y
No affiliation info available
Kang JY
No affiliation info available
Song HE
No affiliation info available
Park I
No affiliation info available
Cho C
No affiliation info available
Fukuoka S
No affiliation info available
Eom SH
No affiliation info available

MeSH

AnimalsCatalytic DomainCrystallography, X-RayDNA, ComplementaryHelicobacter pyloriHumansKidneyModels, MolecularMycobacterium tuberculosisNicotinamide MononucleotidePentosyltransferasesProtein Interaction Domains and MotifsProtein MultimerizationSpecies SpecificityStructural Homology, ProteinSwine

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23626766

Citation

Youn, Hyung-Seop, et al. "Crystal Structure of Sus Scrofa Quinolinate Phosphoribosyltransferase in Complex With Nicotinate Mononucleotide." PloS One, vol. 8, no. 4, 2013, pp. e62027.
Youn HS, Kim MK, Kang GB, et al. Crystal structure of Sus scrofa quinolinate phosphoribosyltransferase in complex with nicotinate mononucleotide. PLoS One. 2013;8(4):e62027.
Youn, H. S., Kim, M. K., Kang, G. B., Kim, T. G., Lee, J. G., An, J. Y., Park, K. R., Lee, Y., Kang, J. Y., Song, H. E., Park, I., Cho, C., Fukuoka, S., & Eom, S. H. (2013). Crystal structure of Sus scrofa quinolinate phosphoribosyltransferase in complex with nicotinate mononucleotide. PloS One, 8(4), e62027. https://doi.org/10.1371/journal.pone.0062027
Youn HS, et al. Crystal Structure of Sus Scrofa Quinolinate Phosphoribosyltransferase in Complex With Nicotinate Mononucleotide. PLoS One. 2013;8(4):e62027. PubMed PMID: 23626766.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of Sus scrofa quinolinate phosphoribosyltransferase in complex with nicotinate mononucleotide. AU - Youn,Hyung-Seop, AU - Kim,Mun-Kyoung, AU - Kang,Gil Bu, AU - Kim,Tae Gyun, AU - Lee,Jung-Gyu, AU - An,Jun Yop, AU - Park,Kyoung Ryoung, AU - Lee,Youngjin, AU - Kang,Jung Youn, AU - Song,Hye-Eun, AU - Park,Inju, AU - Cho,Chunghee, AU - Fukuoka,Shin-Ichi, AU - Eom,Soo Hyun, Y1 - 2013/04/23/ PY - 2012/12/10/received PY - 2013/03/17/accepted PY - 2013/4/30/entrez PY - 2013/4/30/pubmed PY - 2013/12/16/medline SP - e62027 EP - e62027 JF - PloS one JO - PLoS One VL - 8 IS - 4 N2 - We have determined the crystal structure of porcine quinolinate phosphoribosyltransferase (QAPRTase) in complex with nicotinate mononucleotide (NAMN), which is the first crystal structure of a mammalian QAPRTase with its reaction product. The structure was determined from protein obtained from the porcine kidney. Because the full protein sequence of porcine QAPRTase was not available in either protein or nucleotide databases, cDNA was synthesized using reverse transcriptase-polymerase chain reaction to determine the porcine QAPRTase amino acid sequence. The crystal structure revealed that porcine QAPRTases have a hexameric structure that is similar to other eukaryotic QAPRTases, such as the human and yeast enzymes. However, the interaction between NAMN and porcine QAPRTase was different from the interaction found in prokaryotic enzymes, such as those of Helicobacter pylori and Mycobacterium tuberculosis. The crystal structure of porcine QAPRTase in complex with NAMN provides a structural framework for understanding the unique properties of the mammalian QAPRTase active site and designing new antibiotics that are selective for the QAPRTases of pathogenic bacteria, such as H. pylori and M. tuberculosis. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/23626766/Crystal_structure_of_Sus_scrofa_quinolinate_phosphoribosyltransferase_in_complex_with_nicotinate_mononucleotide_ L2 - https://dx.plos.org/10.1371/journal.pone.0062027 DB - PRIME DP - Unbound Medicine ER -