메뉴 건너뛰기




Volumn 46, Issue 2, 2002, Pages 206-214

Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 Å resolution: Specific interactions at subunit interfaces

Author keywords

Crystal structure; Inter subunit interactions; Lactate dehydrogenase; Lactobacillus pentosus; Non allosteric enzyme; Shape complementarity; Structure function relationship; X ray crystallography

Indexed keywords

LACTATE DEHYDROGENASE;

EID: 0036467158     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1165     Document Type: Article
Times cited : (21)

References (49)
  • 4
    • 0027402941 scopus 로고
    • Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase
    • (1993) J Mol Biol , vol.230 , pp. 21-27
    • Iwata, S.1    Ohta, T.2
  • 6
    • 0020491515 scopus 로고
    • Crystallization and preliminary crystallographic analysis at low resolution of the allosteric L-lactate dehydrogenase from Lactobacillus casei
    • (1982) J Mol Biol , vol.162 , pp. 819-838
    • Buehner, M.1    Hecht, H.-J.2
  • 13
    • 0017577897 scopus 로고
    • Comparative studies of lactic acid dehydrogenases in lactic acid bacteria: I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus
    • (1977) Arch Microbiol , vol.112 , pp. 81-93
    • Hensel, R.1    Mayr, U.2    Stetter, K.O.3    Kandler, O.4
  • 15
    • 0019123201 scopus 로고
    • Factors affecting the quaternary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei and Lactobacillus curvatus as investigated by hybridization and ultracentrifugation
    • (1980) Eur J Biochem , vol.110 , pp. 527-538
    • Mayr, U.1    Hensel, R.2    Kandler, O.3
  • 16
    • 0029263306 scopus 로고
    • Role of histidine 188 in fructose 1,6-bisphosphate- and divalent cation-regulated L-lactate dehydrogenase of Lactobacillus casei
    • (1995) Biosci Biotech Biochem , vol.59 , pp. 451-458
    • Taguchi, H.1    Ohta, T.2
  • 17
    • 0023943953 scopus 로고
    • Identification of an allosteric site residue of a fructose 1,6-bisphosphate-dependent L-lactate dehydrogenase of Thermus caldophilus GK24: Production of a non-allosteric form by protein engineering
    • (1988) FEBS Lett , vol.233 , pp. 375-378
    • Matsuzawa, H.1    Machida, M.2    Kunai, K.3    Ito, Y.4    Ohta, T.5
  • 19
    • 0021743361 scopus 로고
    • L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence
    • (1984) Eur J Biochem , vol.145 , pp. 283-290
    • Taguchi, H.1    Matsuzawa, H.2    Ohta, T.3
  • 25
    • 0032579247 scopus 로고    scopus 로고
    • Homotropic activation via the subunit interaction and allosteric symmetry revealed on analysis of hybrid enzymes of L-lactate dehydrogenase
    • (1998) J Biol Chem , vol.273 , pp. 2971-2976
    • Fushinobu, S.1    Ohta, T.2    Matsuzawa, H.3
  • 26
    • 0025779127 scopus 로고
    • D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum
    • (1991) J Biol Chem , vol.266 , pp. 12588-12594
    • Taguchi, H.1    Ohta, T.2
  • 27
    • 0026437845 scopus 로고
    • Unusual amino acid substitution in the anion-binding site of Lactobacillus plantarum non-allosteric L-lactate dehydrogenase
    • (1992) Eur J Biochem , vol.209 , pp. 993-998
    • Taguchi, H.1    Ohta, T.2
  • 31
    • 2042481602 scopus 로고
    • Fast Fourier translation functions
    • Dodson EJ, Gover S, Wolf W, editors. CCP4 Daresbury Study Weekend, nos. DL/SCI/R33, ISSN 0144-5677. Warrington WA4 4AD, UK: Daresbury Laboratory
    • (1992) Molecular Replacement
    • Tickle, I.J.1
  • 32
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project, Number 4) suite: Programs for protein crystallography
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 34
    • 0000449646 scopus 로고
    • Improvement of macromolecular electrondensity maps by the simultaneous application of real and reciprocal space constraints
    • (1993) Acta Cryst , vol.D49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 35
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • (1994) J Mol Biol , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 44
    • 0024846203 scopus 로고
    • The structure of interfaces between subunits of dimeric and tetrameric proteins
    • (1989) Prot Eng , vol.3 , pp. 77-83
    • Miller, S.1
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.