Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima

被引:34
作者
Wang, WR
Kim, R
Yokota, H
Kim, SH [1 ]
机构
[1] Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley Struct Genom Ctr, Phys Biosci Div, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA
关键词
D O I
10.1002/prot.20207
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
[No abstract available]
引用
收藏
页码:246 / 248
页数:3
相关论文
共 14 条
[1]   Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold [J].
Bauer, S ;
Kemter, K ;
Bacher, A ;
Huber, R ;
Fischer, M ;
Steinbacher, S .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 326 (05) :1463-1473
[2]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[3]  
Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254
[4]   Structure of nicotinamide mononucleotide adenylyltransferase:: a key enzyme in NAD+ biosynthesis [J].
D'Angelo, I ;
Raffaelli, N ;
Dabusti, V ;
Lorenzi, T ;
Magni, G ;
Rizzi, M .
STRUCTURE, 2000, 8 (09) :993-1004
[5]   The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity [J].
Izard, T ;
Geerlof, A .
EMBO JOURNAL, 1999, 18 (08) :2021-2030
[6]   SPARSE-MATRIX SAMPLING - A SCREENING METHOD FOR CRYSTALLIZATION OF PROTEINS [J].
JANCARIK, J ;
KIM, SH .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1991, 24 :409-411
[7]   IMPROVED METHODS FOR BUILDING PROTEIN MODELS IN ELECTRON-DENSITY MAPS AND THE LOCATION OF ERRORS IN THESE MODELS [J].
JONES, TA ;
ZOU, JY ;
COWAN, SW ;
KJELDGAARD, M .
ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :110-119
[8]  
MANSTEIN DJ, 1986, J BIOL CHEM, V261, P6169
[9]  
MERRILL AH, 1980, J BIOL CHEM, V255, P1335
[10]   Refinement of macromolecular structures by the maximum-likelihood method [J].
Murshudov, GN ;
Vagin, AA ;
Dodson, EJ .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1997, 53 :240-255