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This study defines the evolutionary relationship between the sulfur incorporation step during Moco biosynthesis and the mechanism of ubiquitin activation.
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Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 8:2001;42-46. This study defines the evolutionary relationship between the sulfur incorporation step during Moco biosynthesis and the mechanism of ubiquitin activation.
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Nat Struct Biol
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Rudolph, M.J.1
Wuebbens, M.M.2
Rajagopalan, K.V.3
Schindelin, H.4
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48
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0035816219
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The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway
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Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R., Matte A., Cygler M. The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J Mol Biol. 310:2001;419-431.
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(2001)
J Mol Biol
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Schrag, J.D.1
Huang, W.2
Sivaraman, J.3
Smith, C.4
Plamondon, J.5
Larocque, R.6
Matte, A.7
Cygler, M.8
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49
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0035860322
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Crystal structures of human gephyrin and plant Cnx1 G domains: Comparative analysis and functional implications
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Schwarz G., Schrader N., Mendel R.R., Hecht H.J., Schindelin H. Crystal structures of human gephyrin and plant Cnx1 G domains: comparative analysis and functional implications. J Mol Biol. 312:2001;405-418.
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(2001)
J Mol Biol
, vol.312
, pp. 405-418
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Schwarz, G.1
Schrader, N.2
Mendel, R.R.3
Hecht, H.J.4
Schindelin, H.5
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50
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0035816706
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X-ray crystal structure of the trimeric N-terminal domain of gephyrin
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Sola M., Kneussel M., Heck I.S., Betz H., Weissenhorn W. X-ray crystal structure of the trimeric N-terminal domain of gephyrin. J Biol Chem. 276:2001;25294-25301.
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(2001)
J Biol Chem
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, pp. 25294-25301
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Sola, M.1
Kneussel, M.2
Heck, I.S.3
Betz, H.4
Weissenhorn, W.5
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51
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0034435586
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Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution
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Stevenson C.E., Sargent F., Buchanan G., Palmer T., Lawson D.M. Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Struct Fold Des. 8:2000;1115-1125.
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(2000)
Struct Fold Des
, vol.8
, pp. 1115-1125
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Stevenson, C.E.1
Sargent, F.2
Buchanan, G.3
Palmer, T.4
Lawson, D.M.5
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52
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0034661492
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Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC
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Wuebbens M.M., Liu M.T., Rajagopalan K., Schindelin H. Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Struct Fold Des. 8:2000;709-718.
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(2000)
Struct Fold Des
, vol.8
, pp. 709-718
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Wuebbens, M.M.1
Liu, M.T.2
Rajagopalan, K.3
Schindelin, H.4
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53
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0034880831
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The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin
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The authors incorporate the structural data on MogA and MoeA to postulate a model for the hexagonal scaffold formed by gephyrin.
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Xiang S., Nichols J., Rajagopalan K.V., Schindelin H. The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure. 9:2001;299-310. The authors incorporate the structural data on MogA and MoeA to postulate a model for the hexagonal scaffold formed by gephyrin.
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(2001)
Structure
, vol.9
, pp. 299-310
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Xiang, S.1
Nichols, J.2
Rajagopalan, K.V.3
Schindelin, H.4
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54
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0035282866
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Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
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Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29:2001;1097-1106.
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(2001)
Nucleic Acids Res
, vol.29
, pp. 1097-1106
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Sofia, H.J.1
Chen, G.2
Hetzler, B.G.3
Reyes-Spindola, J.F.4
Miller, N.E.5
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55
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0034792676
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Radical mechanisms of S-adenosylmethionine-dependent enzymes
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Frey P.A., Booker S.J. Radical mechanisms of S-adenosylmethionine-dependent enzymes. Adv Protein Chem. 58:2001;1-45.
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(2001)
Adv Protein Chem
, vol.58
, pp. 1-45
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Frey, P.A.1
Booker, S.J.2
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56
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0035170874
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Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
-
This study defines the evolutionary relationship between the sulfur incorporation step during thiamine biosynthesis and the mechanism of ubiquitin activation.
-
Wang C., Xi J., Begley T.P., Nicholson L.K. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat Struct Biol. 8:2001;47-51. This study defines the evolutionary relationship between the sulfur incorporation step during thiamine biosynthesis and the mechanism of ubiquitin activation.
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(2001)
Nat Struct Biol
, vol.8
, pp. 47-51
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-
Wang, C.1
Xi, J.2
Begley, T.P.3
Nicholson, L.K.4
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57
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0035933851
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A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli
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Leimkuhler S., Rajagopalan K.V. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 276:2001;22024-22031.
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(2001)
J Biol Chem
, vol.276
, pp. 22024-22031
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Leimkuhler, S.1
Rajagopalan, K.V.2
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58
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0037022788
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Structure of FAD-bound L-aspartate oxidase: Insight into substrate specificity and catalysis
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This paper provides important observations for understanding the catalytic mechanism of LASPO with relevance to the succinate dehydrogenase/fumarate reductase family.
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Bossi R.T., Negri A., Tedeschi G., Mattevi A. Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry. 41:2002;3018-3024. This paper provides important observations for understanding the catalytic mechanism of LASPO with relevance to the succinate dehydrogenase/fumarate reductase family.
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(2002)
Biochemistry
, vol.41
, pp. 3018-3024
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Bossi, R.T.1
Negri, A.2
Tedeschi, G.3
Mattevi, A.4
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59
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0001406338
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Structure of L-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
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Mattevi A., Tedeschi G., Bacchella L., Coda A., Negri A., Ronchi S. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Struct Fold Des. 7:1999;745-756.
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(1999)
Struct Fold Des
, vol.7
, pp. 745-756
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Mattevi, A.1
Tedeschi, G.2
Bacchella, L.3
Coda, A.4
Negri, A.5
Ronchi, S.6
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60
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0034141264
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Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase
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Ceciliani F., Caramori T., Ronchi S., Tedeschi G., Mortarino M., Galizzi A. Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase. Protein Expr Purif. 18:2000;64-70.
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(2000)
Protein Expr Purif
, vol.18
, pp. 64-70
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Ceciliani, F.1
Caramori, T.2
Ronchi, S.3
Tedeschi, G.4
Mortarino, M.5
Galizzi, A.6
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61
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0031568330
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A new function for a common fold: The crystal structure of quinolinic acid phosphoribosyltransferase
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Eads J.C., Ozturk D., Wexler T.B., Grubmeyer C., Sacchettini J.C. A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Structure. 5:1997;47-58.
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(1997)
Structure
, vol.5
, pp. 47-58
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Eads, J.C.1
Ozturk, D.2
Wexler, T.B.3
Grubmeyer, C.4
Sacchettini, J.C.5
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62
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0032534756
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Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: A potential TB drug target
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Sharma V., Grubmeyer C., Sacchettini J.C. Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target. Structure. 6:1998;1587-1599.
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(1998)
Structure
, vol.6
, pp. 1587-1599
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Sharma, V.1
Grubmeyer, C.2
Sacchettini, J.C.3
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63
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0037031886
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Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenylyltransferase and ribosylnicotinamide kinase activities
-
Singh S.K., Kurnasov O.V., Chen B., Robinson H., Grishin N.V., Osterman A., Zhang H. Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenylyltransferase and ribosylnicotinamide kinase activities. J Biol Chem. 277:2002;33291-33299.
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(2002)
J Biol Chem
, vol.277
, pp. 33291-33299
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Singh, S.K.1
Kurnasov, O.V.2
Chen, B.3
Robinson, H.4
Grishin, N.V.5
Osterman, A.6
Zhang, H.7
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64
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0034665459
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+ biosynthesis
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This paper reports the first structure of a NMNAT, that is, M. jannaschii NMNAT in complex with ATP. The analysis of the ATP-binding site allowed the assignment of NMNAT to a wide family of nucleotidyltransferase α/β phosphodiesterases.
-
+ biosynthesis. Struct Fold Des. 8:2000;993-1004. This paper reports the first structure of a NMNAT, that is, M. jannaschii NMNAT in complex with ATP. The analysis of the ATP-binding site allowed the assignment of NMNAT to a wide family of nucleotidyltransferase α/β phosphodiesterases.
-
(2000)
Struct Fold Des
, vol.8
, pp. 993-1004
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-
D'Angelo, I.1
Raffaelli, N.2
Dabusti, V.3
Lorenzi, T.4
Magni, G.5
Rizzi, M.6
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65
-
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0037040970
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Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis
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This paper describes the structure of human NMNAT, a target for cancer chemotherapy, in its free form. Structural comparison with other NMNATs revealed the minimal structural framework for ATP binding in all NMNATs.
-
Garavaglia S., D'Angelo I., Emanuelli M., Carnevali F., Pierella F., Magni G., Rizzi M. Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis. J Biol Chem. 277:2002;8524-8530. This paper describes the structure of human NMNAT, a target for cancer chemotherapy, in its free form. Structural comparison with other NMNATs revealed the minimal structural framework for ATP binding in all NMNATs.
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(2002)
J Biol Chem
, vol.277
, pp. 8524-8530
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-
Garavaglia, S.1
D'Angelo, I.2
Emanuelli, M.3
Carnevali, F.4
Pierella, F.5
Magni, G.6
Rizzi, M.7
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66
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0036479316
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Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase
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Olland A.M., Underwood K.W., Czerwinski R.M., Lo M.C., Aulabaugh A., Bard J., Stahl M.L., Somers W.S., Sullivan F.X., Chopra R. Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase. J Biol Chem. 277:2002;3698-3707.
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(2002)
J Biol Chem
, vol.277
, pp. 3698-3707
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-
Olland, A.M.1
Underwood, K.W.2
Czerwinski, R.M.3
Lo, M.C.4
Aulabaugh, A.5
Bard, J.6
Stahl, M.L.7
Somers, W.S.8
Sullivan, F.X.9
Chopra, R.10
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67
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0036153602
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Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD
-
The structural bases for the exquisite preference of eubacterial NMNAT for the acid form of the mononucleotide are revealed by the structural analysis described in this paper.
-
Zhang H., Zhou T., Kurnasov O., Cheek S., Grishin N.V., Osterman A. Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD. Structure. 10:2002;69-79. The structural bases for the exquisite preference of eubacterial NMNAT for the acid form of the mononucleotide are revealed by the structural analysis described in this paper.
-
(2002)
Structure
, vol.10
, pp. 69-79
-
-
Zhang, H.1
Zhou, T.2
Kurnasov, O.3
Cheek, S.4
Grishin, N.V.5
Osterman, A.6
-
68
-
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0035831542
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+ synthesis: Structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes
-
The structure of M. thermoautotrophicum NMNAT in complex with NAD reported in this paper reveals the structural determinants for recognition of NMN by archaeal NMNATs.
-
+ synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes. J Biol Chem. 276:2001;7225-7232. The structure of M. thermoautotrophicum NMNAT in complex with NAD reported in this paper reveals the structural determinants for recognition of NMN by archaeal NMNATs.
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(2001)
J Biol Chem
, vol.276
, pp. 7225-7232
-
-
Saridakis, V.1
Christendat, D.2
Kimber, M.S.3
Dharamsi, A.4
Edwards, A.M.5
Pai, E.F.6
-
69
-
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0037066769
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Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin
-
This paper contains an extensive structural study on human NMNAT, including the structure of a complex with a metabolite of a potent antineoplastic agent. Structural bases for the dual specificity shown by the human enzyme are described.
-
Zhou T., Kurnasov O., Tomchick D.R., Binns D.D., Grishin N.V., Marquez V.E., Osterman A.L., Zhang H. Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin. J Biol Chem. 277:2002;13148-13154. This paper contains an extensive structural study on human NMNAT, including the structure of a complex with a metabolite of a potent antineoplastic agent. Structural bases for the dual specificity shown by the human enzyme are described.
-
(2002)
J Biol Chem
, vol.277
, pp. 13148-13154
-
-
Zhou, T.1
Kurnasov, O.2
Tomchick, D.R.3
Binns, D.D.4
Grishin, N.V.5
Marquez, V.E.6
Osterman, A.L.7
Zhang, H.8
-
70
-
-
0037051999
-
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN
-
Werner E., Ziegler M., Lerner F., Schweiger M., Heinemann U. Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN. FEBS Lett. 516:2002;239-244.
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(2002)
FEBS Lett
, vol.516
, pp. 239-244
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-
Werner, E.1
Ziegler, M.2
Lerner, F.3
Schweiger, M.4
Heinemann, U.5
-
71
-
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0034984827
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+ synthetase from Bacillus subtilis
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+ synthetase from Bacillus subtilis. Acta Crystallogr D Biol Crystallogr. 57:2001;806-812.
-
(2001)
Acta Crystallogr D Biol Crystallogr
, vol.57
, pp. 806-812
-
-
Devedjiev, Y.1
Symersky, J.2
Singh, R.3
Jedrzejas, M.4
Brouillette, C.5
Brouillette, W.6
Muccio, D.7
Chattopadhyay, D.8
DeLucas, L.9
-
74
-
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0035997123
-
+ synthetase from Bacillus subtilis at 1 Å resolution
-
This paper describes the structure at very high resolution of B. subtilis NADS in complex with the adenylate-NAD reaction intermediate. The structure was already reported in a previous paper [72], but the atomic resolution reached in this study allows the authors to propose a possible mechanism for the second step of the overall reaction.
-
+ synthetase from Bacillus subtilis at 1 Å resolution. Acta Crystallogr D Biol Crystallogr. 58:2002;1138-1146. This paper describes the structure at very high resolution of B. subtilis NADS in complex with the adenylate-NAD reaction intermediate. The structure was already reported in a previous paper [72], but the atomic resolution reached in this study allows the authors to propose a possible mechanism for the second step of the overall reaction.
-
(2002)
Acta Crystallogr D Biol Crystallogr
, vol.58
, pp. 1138-1146
-
-
Symersky, J.1
Devedjiev, Y.2
Moore, K.3
Brouillette, C.4
DeLucas, L.5
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