메뉴 건너뛰기




Volumn 349, Issue 1, 2005, Pages 61-72

Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme

Author keywords

7,8 dihydroneopterin aldolase; Allosteric regulation; Mycobacterium tuberculosis; Tetrahydrofolate biosynthesis; X ray crystallography

Indexed keywords

7,8 DIHYDRONEOPTERIN ALDOLASE; ANTIOXIDANT; BACTERIAL ENZYME; FOLIC ACID; METHYL GROUP; NEOPTERIN; TETRAMER; UNCLASSIFIED DRUG;

EID: 18144410535     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.023     Document Type: Article
Times cited : (39)

References (24)
  • 3
    • 0034664991 scopus 로고    scopus 로고
    • Tetrahydrofolate and tetrahydromethanopterin compared: Functionally distinct carriers in C1 metabolism
    • B.E. Maden Tetrahydrofolate and tetrahydromethanopterin compared: functionally distinct carriers in C1 metabolism Biochem. J. 350 2000 609 629
    • (2000) Biochem. J. , vol.350 , pp. 609-629
    • Maden, B.E.1
  • 6
    • 0032504243 scopus 로고    scopus 로고
    • Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase
    • C. Haussmann, F. Rohdich, E. Schmidt, A. Bacher, and G. Richter Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase J. Biol. Chem. 273 1998 17418 17424
    • (1998) J. Biol. Chem. , vol.273 , pp. 17418-17424
    • Haussmann, C.1    Rohdich, F.2    Schmidt, E.3    Bacher, A.4    Richter, G.5
  • 7
    • 0032066057 scopus 로고    scopus 로고
    • Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus
    • M. Hennig, A. D'Arcy, I.C. Hampele, M.G. Page, C. Oefner, and G.E. Dale Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus Nature Struct. Biol. 5 1998 357 362
    • (1998) Nature Struct. Biol. , vol.5 , pp. 357-362
    • Hennig, M.1    D'Arcy, A.2    Hampele, I.C.3    Page, M.G.4    Oefner, C.5    Dale, G.E.6
  • 8
    • 2542490230 scopus 로고    scopus 로고
    • Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class
    • S. Bauer, A.K. Schott, V. Illarionova, A. Bacher, R. Huber, and M. Fischer Biosynthesis of tetrahydrofolate in plants: crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class J. Mol. Biol. 339 2004 967 979
    • (2004) J. Mol. Biol. , vol.339 , pp. 967-979
    • Bauer, S.1    Schott, A.K.2    Illarionova, V.3    Bacher, A.4    Huber, R.5    Fischer, M.6
  • 9
    • 0032544213 scopus 로고    scopus 로고
    • Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii
    • M.C. Thomas, S.P. Ballantine, S.S. Bethell, S. Bains, P. Kellam, and C.J. Delves Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii Biochemistry 37 1998 11629 11636
    • (1998) Biochemistry , vol.37 , pp. 11629-11636
    • Thomas, M.C.1    Ballantine, S.P.2    Bethell, S.S.3    Bains, S.4    Kellam, P.5    Delves, C.J.6
  • 10
    • 0017138398 scopus 로고
    • Oxygenation-linked subunit interactions in human hemoglobin: Experimental studies on the concentration dependence of oxygenation curves
    • F.C. Mills, M.L. Johnson, and G.K. Ackers Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves Biochemistry 15 1976 5350 5362
    • (1976) Biochemistry , vol.15 , pp. 5350-5362
    • Mills, F.C.1    Johnson, M.L.2    Ackers, G.K.3
  • 11
    • 0020640999 scopus 로고
    • Purification, properties and assay of d-ribulose 5-phosphate 3-epimerase from human erythrocytes
    • A. Karmali, A.F. Drake, and N. Spencer Purification, properties and assay of d-ribulose 5-phosphate 3-epimerase from human erythrocytes Biochem. J. 211 1983 617 623
    • (1983) Biochem. J. , vol.211 , pp. 617-623
    • Karmali, A.1    Drake, A.F.2    Spencer, N.3
  • 12
    • 0037135712 scopus 로고    scopus 로고
    • Protein and thiol oxidation in cells exposed to peroxyl radicals is inhibited by the macrophage synthesised pterin 7,8-dihydroneopterin
    • S. Duggan, C. Rait, A. Platt, and S. Gieseg Protein and thiol oxidation in cells exposed to peroxyl radicals is inhibited by the macrophage synthesised pterin 7,8-dihydroneopterin Biochim. Biophys. Acta 1591 2002 139 145
    • (2002) Biochim. Biophys. Acta , vol.1591 , pp. 139-145
    • Duggan, S.1    Rait, C.2    Platt, A.3    Gieseg, S.4
  • 13
    • 0037527725 scopus 로고    scopus 로고
    • Induction of apoptosis in human blood T cells by 7,8-dihydroneopterin: The difference between healthy controls and patients with systemic lupus erythematosus
    • B. Wirleitner, G. Obermoser, G. Bock, G. Neurauter, H. Schennach, N. Sepp, and D. Fuchs Induction of apoptosis in human blood T cells by 7,8-dihydroneopterin: the difference between healthy controls and patients with systemic lupus erythematosus Clin. Immunol. 107 2003 152 159
    • (2003) Clin. Immunol. , vol.107 , pp. 152-159
    • Wirleitner, B.1    Obermoser, G.2    Bock, G.3    Neurauter, G.4    Schennach, H.5    Sepp, N.6    Fuchs, D.7
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter R.M. Sweet Methods in Enzymology vol. 276 1996 Academic Press New York
    • (1996) Methods in Enzymology , vol.276
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta. Crystallog. sect. A 47 1991 110 119
    • (1991) Acta. Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • R.A. Laskowski, D.S. Moss, and J.M. Thornton Main-chain bond lengths and bond angles in protein structures J. Mol. Biol. 231 1993 1049 1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 21
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • C. Colovos, and T.O. Yeates Verification of protein structures: patterns of nonbonded atomic interactions Protein Sci. 2 1993 1511 1519
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 22
    • 0037378351 scopus 로고    scopus 로고
    • The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)
    • C. Mura, A. Kozhukhovsky, M. Gingery, M. Phillips, and D. Eisenberg The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs) Protein Sci. 12 2003 832 847
    • (2003) Protein Sci. , vol.12 , pp. 832-847
    • Mura, C.1    Kozhukhovsky, A.2    Gingery, M.3    Phillips, M.4    Eisenberg, D.5
  • 23
    • 12144288664 scopus 로고    scopus 로고
    • Discovery of potent inhibitors of dihydroneopterin aldolase using CrystaLEAD high-throughput X-ray crystallographic screening and structure-directed lead optimization
    • W.J. Sanders, V.L. Nienaber, C.G. Lerner, J.O. McCall, S.M. Merrick, and S.J. Swanson Discovery of potent inhibitors of dihydroneopterin aldolase using CrystaLEAD high-throughput X-ray crystallographic screening and structure-directed lead optimization J. Med. Chem. 47 2004 1709 1718
    • (2004) J. Med. Chem. , vol.47 , pp. 1709-1718
    • Sanders, W.J.1    Nienaber, V.L.2    Lerner, C.G.3    McCall, J.O.4    Merrick, S.M.5    Swanson, S.J.6
  • 24
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • I.N. Shindyalov, and P.E. Bourne Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng. 11 1998 739 747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.