메뉴 건너뛰기




Volumn 21, Issue 11, 2014, Pages 1013-1015

Crystal structure of the vitamin B 3 transporter PnuC, a full-length SWEET homolog

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; NICOTINAMIDE; NICOTINAMIDE RIBOSIDE; PROTEIN PNUC; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; NICOTINAMIDE-BETA-RIBOSIDE; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84908869634     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2909     Document Type: Article
Times cited : (36)

References (27)
  • 1
    • 0034968382 scopus 로고    scopus 로고
    • NadN and e (P4) are essential for utilization of NAD and nicotinamide mononucleotide but not nicotinamide riboside in Haemophilus influenzae
    • Kemmer, G. et al. NadN and e (P4) are essential for utilization of NAD and nicotinamide mononucleotide but not nicotinamide riboside in Haemophilus influenzae. J. Bacteriol. 183, 3974-3981 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 3974-3981
    • Kemmer, G.1
  • 2
    • 21144437936 scopus 로고    scopus 로고
    • Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica
    • Grose, J.H. et al. Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica. J. Bacteriol. 187, 4521-4530 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 4521-4530
    • Grose, J.H.1
  • 3
    • 41849131511 scopus 로고    scopus 로고
    • Transcriptional regulation of NAD metabolism in bacteria: Genomic reconstruction of NiaR (YrxA) regulon
    • Rodionov, D.A. et al. Transcriptional regulation of NAD metabolism in bacteria: genomic reconstruction of NiaR (YrxA) regulon. Nucleic Acids Res. 36, 2032-2046 (2008).
    • (2008) Nucleic Acids Res , vol.36 , pp. 2032-2046
    • Rodionov, D.A.1
  • 4
    • 21144447964 scopus 로고    scopus 로고
    • Coupling of NAD+ biosynthesis and nicotinamide ribosyl transport: Characterization of NadR ribonucleotide kinase mutants of Haemophilus influenzae
    • Merdanovic, M., Sauer, E. &Reidl, J. Coupling of NAD+ biosynthesis and nicotinamide ribosyl transport: characterization of NadR ribonucleotide kinase mutants of Haemophilus influenzae. J. Bacteriol. 187, 4410-4420 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 4410-4420
    • Merdanovic, M.1    Sauer, E.2    Reidl, J.3
  • 5
    • 0041823287 scopus 로고    scopus 로고
    • Nicotinamide ribosyl uptake mutants in Haemophilus influenzae
    • Herbert, M. et al. Nicotinamide ribosyl uptake mutants in Haemophilus influenzae. Infect. Immun. 71, 5398-5401 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 5398-5401
    • Herbert, M.1
  • 6
    • 33749347331 scopus 로고    scopus 로고
    • NAD+ utilization in Pasteurellaceae: Simplification of a complex pathway
    • Gerlach, G. &Reidl, J. NAD+ utilization in Pasteurellaceae: simplification of a complex pathway. J. Bacteriol. 188, 6719-6727 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 6719-6727
    • Gerlach, G.1    Reidl, J.2
  • 7
    • 78649481757 scopus 로고    scopus 로고
    • Sugar transporters for intercellular exchange and nutrition of pathogens
    • Chen, L.-Q. et al. Sugar transporters for intercellular exchange and nutrition of pathogens. Nature 468, 527-532 (2010).
    • (2010) Nature , vol.468 , pp. 527-532
    • Chen, L.-Q.1
  • 8
    • 84886599277 scopus 로고    scopus 로고
    • The transporter-opsin-G protein-coupled receptor (TOG) superfamily
    • Yee, D.C. et al. The transporter-opsin-G protein-coupled receptor (TOG) superfamily. FEBS J. 280, 5780-5800 (2013).
    • (2013) FEBS J , vol.280 , pp. 5780-5800
    • Yee, D.C.1
  • 9
    • 84875153197 scopus 로고    scopus 로고
    • Glucose transport families SLC5 and SLC50
    • Wright, E.M. Glucose transport families SLC5 and SLC50. Mol. Aspects Med. 34, 183-196 (2013).
    • (2013) Mol. Aspects Med , vol.34 , pp. 183-196
    • Wright, E.M.1
  • 10
    • 84899484320 scopus 로고    scopus 로고
    • Nectar secretion requires sucrose phosphate synthases and the sugar transporter SWEET9
    • Lin, I.W. et al. Nectar secretion requires sucrose phosphate synthases and the sugar transporter SWEET9. Nature 508, 546-549 (2014).
    • (2014) Nature , vol.508 , pp. 546-549
    • Lin, I.W.1
  • 11
    • 84855846270 scopus 로고    scopus 로고
    • Sucrose efflux mediated by SWEET proteins as a key step for phloem transport
    • Chen, L.-Q. et al. Sucrose efflux mediated by SWEET proteins as a key step for phloem transport. Science 335, 207-211 (2012).
    • (2012) Science , vol.335 , pp. 207-211
    • Chen, L.-Q.1
  • 12
    • 84884604210 scopus 로고    scopus 로고
    • Functional role of oligomerization for bacterial and plant SWEET sugar transporter family
    • Xuan, Y.H. et al. Functional role of oligomerization for bacterial and plant SWEET sugar transporter family. Proc. Natl. Acad. Sci. USA 110, E3685-E3694 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E3685-E3694
    • Xuan, Y.H.1
  • 13
    • 84911473884 scopus 로고    scopus 로고
    • Structures of bacterial homologues of SWEET transporters in two distinct conformations
    • doi:10.1038/nature13670 3 September 2014
    • Xu, Y. et al. Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature doi:10.1038/nature13670 (3 September 2014).
    • Nature
    • Xu, Y.1
  • 14
  • 15
    • 32244436490 scopus 로고    scopus 로고
    • Identification and evolution of dual-topology membrane proteins
    • Rapp, M., Granseth, E., Seppl, S. &von Heijne, G. Identification and evolution of dual-topology membrane proteins. Nat. Struct. Mol. Biol. 13, 112-116 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 112-116
    • Rapp, M.1    Granseth, E.2    Seppl, S.3    Von Heijne, G.4
  • 16
    • 84872781515 scopus 로고    scopus 로고
    • Structural biology: (pseudo-)symmetrical transport
    • Forrest, L.R. Structural biology: (pseudo-)symmetrical transport. Science 339, 399-401 (2013).
    • (2013) Science , vol.339 , pp. 399-401
    • Forrest, L.R.1
  • 17
    • 9644301034 scopus 로고    scopus 로고
    • PnuC and the utilization of the nicotinamide riboside analog 3-aminopyridine in Haemophilus influenzae
    • Sauer, E., Merdanovic, M., Mortimer, A.P., Bringmann, G. &Reidl, J. PnuC and the utilization of the nicotinamide riboside analog 3-aminopyridine in Haemophilus influenzae. Antimicrob. Agents Chemother. 48, 4532-4541 (2004).
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 4532-4541
    • Sauer, E.1    Merdanovic, M.2    Mortimer, A.P.3    Bringmann, G.4    Reidl, J.5
  • 18
    • 82455188342 scopus 로고    scopus 로고
    • RibM from Streptomyces davawensis is a riboflavin/roseoflavin transporter and may be useful for the optimization of riboflavin production strains
    • Hemberger, S. et al. RibM from Streptomyces davawensis is a riboflavin/roseoflavin transporter and may be useful for the optimization of riboflavin production strains. BMC Biotechnol. 11, 119 (2011).
    • (2011) BMC Biotechnol , vol.11 , Issue.119
    • Hemberger, S.1
  • 19
    • 84864674576 scopus 로고    scopus 로고
    • Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution
    • Birkner, J.P., Poolman, B. &Koer, A. Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution. Proc. Natl. Acad. Sci. USA 109, 12944-12949 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 12944-12949
    • Birkner, J.P.1    Poolman, B.2    Koer, A.3
  • 20
    • 68849132462 scopus 로고    scopus 로고
    • Selenomethionine incorporation in proteins expressed in Lactococcus lactis
    • Berntsson, R.P.-A. et al. Selenomethionine incorporation in proteins expressed in Lactococcus lactis. Protein Sci. 18, 1121-1127 (2009).
    • (2009) Protein Sci , vol.18 , pp. 1121-1127
    • Berntsson, R.P.-A.1
  • 21
    • 79953143244 scopus 로고    scopus 로고
    • Quaternary structure and functional unit of energy coupling factor (ECF)-type transporters
    • Ter Beek, J., Duurkens, R.H., Erkens, G.B. &Slotboom, D.J. Quaternary structure and functional unit of energy coupling factor (ECF)-type transporters. J. Biol. Chem. 286, 5471-5475 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 5471-5475
    • Ter Beek, J.1    Duurkens, R.H.2    Erkens, G.B.3    Slotboom, D.J.4
  • 22
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom, D.J., Duurkens, R.H., Olieman, K. &Erkens, G.B. Static light scattering to characterize membrane proteins in detergent solution. Methods 46, 73-82 (2008).
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 24
    • 66249112826 scopus 로고    scopus 로고
    • Decision-making in structure solution using Bayesian estimates of map quality: The PHENIX AutoSol wizard
    • Terwilliger, T.C. et al. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard. Acta Crystallogr. D Biol. Crystallogr. 65, 582-601 (2009).
    • (2009) Acta Crystallogr. D Biol. Crystallogr , vol.65 , pp. 582-601
    • Terwilliger, T.C.1
  • 25
    • 37349103121 scopus 로고    scopus 로고
    • Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard
    • Terwilliger, T.C. et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard. Acta Crystallogr. D Biol. Crystallogr. 64, 61-69 (2008).
    • (2008) Acta Crystallogr. D Biol. Crystallogr , vol.64 , pp. 61-69
    • Terwilliger, T.C.1
  • 27
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G.N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011)
    • (2011) Acta Crystallogr. D Biol. Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.