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Volumn 72, Issue 3, 2008, Pages 1066-1070

Crystal structure of a PduO-type ATP:cobalamin adenosyltransferase from Burkholderia thailandensis

Author keywords

Adenosyltransferase; Cobalamin; Helix bundle; Homotrimer

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; COBALAMIN ADENOSYLTRASFERASE;

EID: 47349105036     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22084     Document Type: Article
Times cited : (3)

References (16)
  • 1
    • 0029658689 scopus 로고    scopus 로고
    • Cobalamin (coenzyme B12): Synthesis and biological significance
    • Roth JR, Lawrence JG, Bobik TA. Cobalamin (coenzyme B12): synthesis and biological significance. Annu Rev Microbiol 1996;50:137-181.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 137-181
    • Roth, J.R.1    Lawrence, J.G.2    Bobik, T.A.3
  • 2
    • 0022430394 scopus 로고
    • Mechanisms of coenzyme B12-dependent rearrangements
    • Halpern J. Mechanisms of coenzyme B12-dependent rearrangements. Science 1985;227:869-875.
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 3
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid E, Rappleye C, Stojiljkovic I, Roth J. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. J Bacteriol 1999;181:5317-5329.
    • (1999) J Bacteriol , vol.181 , pp. 5317-5329
    • Kofoid, E.1    Rappleye, C.2    Stojiljkovic, I.3    Roth, J.4
  • 4
    • 0035895343 scopus 로고    scopus 로고
    • Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP
    • Bauer CB, Fonseca MV, Holden HM, Thoden JB, Thompson TB, Escalante-Semerena JC, Rayment I. Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP. Biochemistry 2001;40:361-374.
    • (2001) Biochemistry , vol.40 , pp. 361-374
    • Bauer, C.B.1    Fonseca, M.V.2    Holden, H.M.3    Thoden, J.B.4    Thompson, T.B.5    Escalante-Semerena, J.C.6    Rayment, I.7
  • 6
    • 0142071742 scopus 로고    scopus 로고
    • Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes
    • Rodionov DA, Vitreschak AG, Mironov AA, Gelfand MS. Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes. J Biol Chem 2003;278:41148-41159.
    • (2003) J Biol Chem , vol.278 , pp. 41148-41159
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 8
    • 33845937432 scopus 로고    scopus 로고
    • Structure of ATP-bound human ATP:Cobalamin adenosyltransferase
    • Schubert HL, Hill CP. Structure of ATP-bound human ATP:Cobalamin adenosyltransferase. Biochemistry 2006;45:15188-15196.
    • (2006) Biochemistry , vol.45 , pp. 15188-15196
    • Schubert, H.L.1    Hill, C.P.2
  • 9
    • 34047258871 scopus 로고    scopus 로고
    • Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri
    • Maurice MS, Mera PE, Taranto MP, Sesma F, Escalante-Semerena JC, Rayment I. Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri. J Biol Chem 2007;282:2596-2605.
    • (2007) J Biol Chem , vol.282 , pp. 2596-2605
    • Maurice, M.S.1    Mera, P.E.2    Taranto, M.P.3    Sesma, F.4    Escalante-Semerena, J.C.5    Rayment, I.6
  • 10
    • 34250883841 scopus 로고    scopus 로고
    • Molecular properties of two proteins homologous to PduO-type ATP:cob(I)alamin adenosyltransferase from Sulfolobus tokodaii
    • Tanaka Y, Sasaki T, Kumagai I, Yasutake Y, Yao M, Tanaka I, Tsumoto K. Molecular properties of two proteins homologous to PduO-type ATP:cob(I)alamin adenosyltransferase from Sulfolobus tokodaii. Proteins 2007;68:446-457.
    • (2007) Proteins , vol.68 , pp. 446-457
    • Tanaka, Y.1    Sasaki, T.2    Kumagai, I.3    Yasutake, Y.4    Yao, M.5    Tanaka, I.6    Tsumoto, K.7
  • 11
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 13
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. COOT: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystalogr 2004;60:2126-2132.
    • (2004) Acta Crystallogr D Biol Crystalogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 16
    • 47349084630 scopus 로고    scopus 로고
    • Palo Alto, CA: DeLano Scientific;, available at
    • DeLano WL. The PyMOL molecular graphics system. Palo Alto, CA: DeLano Scientific; 2002 (available at http://pymol.sourceforge.net).
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.