메뉴 건너뛰기




Volumn 79, Issue 4, 2011, Pages 1193-1204

Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima

Author keywords

Active site mutant; Biofuel industry; Catalytic intermediate; Endoglucanase; Hyperthermophile; Mercury derivatives; Synchrotron radiations

Indexed keywords

ARGININE; BACTERIAL ENZYME; CELLOBIOSE; CELLULASE; MERCURY; THERMOTOGA MARITIMA CELLULASE 12A; TYROSINE; UNCLASSIFIED DRUG;

EID: 79952489592     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22953     Document Type: Article
Times cited : (33)

References (28)
  • 2
    • 0028924376 scopus 로고
    • Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials
    • Bronnenmeier K, Kern A, Liebl W, Staudenbauer WL. Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials. Appl Environ Microbiol 1995; 61: 1399-1407.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1399-1407
    • Bronnenmeier, K.1    Kern, A.2    Liebl, W.3    Staudenbauer, W.4
  • 3
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • Liebl W, Ruile P, Bronnenmeier K, Riedel K, Lottspeich F, Greif I. Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes. Microbiology 1996; 142: 2533-2542.
    • (1996) Microbiology , vol.142 , pp. 2533-2542
    • Liebl, W.1    Ruile, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 5
    • 0031430922 scopus 로고    scopus 로고
    • The Streptomyces lividans family 12 endoglucanase: construction of the catalytic core, expression, and X-ray structure at 1.75 A resolution
    • Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ. The Streptomyces lividans family 12 endoglucanase: construction of the catalytic core, expression, and X-ray structure at 1.75 A resolution. Biochemistry 1997; 36: 16032-16039.
    • (1997) Biochemistry , vol.36 , pp. 16032-16039
    • Sulzenbacher, G.1    Shareck, F.2    Morosoli, R.3    Dupont, C.4    Davies, G.5
  • 6
    • 0033551103 scopus 로고    scopus 로고
    • The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution
    • Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ. The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution. Biochemistry 1999; 38: 4826-4833.
    • (1999) Biochemistry , vol.38 , pp. 4826-4833
    • Sulzenbacher, G.1    Mackenzie, L.2    Wilson, K.3    Withers, S.4    Dupont, C.5    Davies, G.6
  • 8
    • 0036300754 scopus 로고    scopus 로고
    • The structure of Rhodothermus marinus endoglucanase Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution
    • Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E. The structure of Rhodothermus marinus endoglucanase Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution. J Mol Biol 2002; 320: 883-897.
    • (2002) J Mol Biol , vol.320 , pp. 883-897
    • Crennell, S.1    Hreggvidsson, G.2    Nordberg Karlsson, E.3
  • 9
    • 30344484545 scopus 로고    scopus 로고
    • Dimerization and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A
    • Crennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E. Dimerization and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A. J Mol Biol 2006; 356: 57-71.
    • (2006) J Mol Biol , vol.356 , pp. 57-71
    • Crennell, S.1    Cook, D.2    Minns, A.3    Svergun, D.4    Andersen, R.5    Nordberg Karlsson, E.6
  • 12
  • 13
    • 4444264058 scopus 로고    scopus 로고
    • Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A
    • Sandgren M, Berglund GI, Shaw A, Ståhlberg J, Kenne L, Desmet T, Mitchinson C. Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A. J Mol Biol 2004; 342: 1505-1517.
    • (2004) J Mol Biol , vol.342 , pp. 1505-1517
    • Sandgren, M.1    Berglund, G.2    Shaw, A.3    Ståhlberg, J.4    Kenne, L.5    Desmet, T.6    Mitchinson, C.7
  • 14
    • 0036005620 scopus 로고    scopus 로고
    • Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride
    • Khademi S, Zhang D, Swanson SM, Wartenberg A, Witte K, Meyer EF. Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride. Acta Crystallogr 2002; D58: 660-667.
    • (2002) Acta Crystallogr , vol.D58 , pp. 660-667
    • Khademi, S.1    Zhang, D.2    Swanson, S.3    Wartenberg, A.4    Witte, K.5    Meyer, E.6
  • 15
    • 20444378957 scopus 로고    scopus 로고
    • Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes
    • Sandgren M, Ståhlberg J, Mitchinson C. Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes. Prog Biophys Mol Biol 2005; 89: 246-291.
    • (2005) Prog Biophys Mol Biol , vol.89 , pp. 246-291
    • Sandgren, M.1    Ståhlberg, J.2    Mitchinson, C.3
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsk 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
    • Otwinowsk, Z.1    Minor, W.2
  • 17
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr 1999; D55: 849-861.
    • (1999) Acta Crystallogr , vol.D55 , pp. 849-861
    • Terwilliger, T.1    Berendzen, J.2
  • 18
    • 0033896691 scopus 로고    scopus 로고
    • Maximum likelihood density modification
    • Terwilliger TC. Maximum likelihood density modification. Acta Crystallogr 2000; D56: 965-972.
    • (2000) Acta Crystallogr , vol.D56 , pp. 965-972
    • Terwilliger, T.1
  • 19
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger TC. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr 2003; D59: 38-44.
    • (2003) Acta Crystallogr , vol.D59 , pp. 38-44
    • Terwilliger, T.1
  • 20
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr 1991; A47: 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.1    Zou, J.2    Cowan, S.3    Kjeldgaard, M.4
  • 22
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • USA: DeLano Scientific LLC.
    • DeLano WL. The PyMOL molecular graphics system. USA: DeLano Scientific LLC; 2008.
    • (2008)
    • Delano, W.1
  • 23
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS. The anatomy and taxonomy of protein structure. Adv Protein Chem 1981; 34: 167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.1
  • 24
    • 0037036704 scopus 로고    scopus 로고
    • Crystal structure and hydrogen-bonding system in cellulose I-beta from synchrotron X-ray and neutron fiber diffraction
    • Nishiyama Y, Langan P, Chanzy H. Crystal structure and hydrogen-bonding system in cellulose I-beta from synchrotron X-ray and neutron fiber diffraction. J Am Chem Soc 2002; 124: 9074-9082.
    • (2002) J Am Chem Soc , vol.124 , pp. 9074-9082
    • Nishiyama, Y.1    Langan, P.2    Chanzy, H.3
  • 27
    • 28044459167 scopus 로고    scopus 로고
    • Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures
    • Sun HY, Ko TP, Kuo CJ, Guo RT, Chou CC, Liang PH, Wang AHJ. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures. J Bacteriol 2005; 187: 8137-8148.
    • (2005) J Bacteriol , vol.187 , pp. 8137-8148
    • Sun, H.1    Ko, T.2    Kuo, C.3    Guo, R.4    Chou, C.5    Liang, P.6    Wang, A.7
  • 28
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: occurrence, biochemistry, functions and applications
    • Rudiger H, Gabius HJ. Plant lectins: occurrence, biochemistry, functions and applications. Glycoconj J 2001; 18: 589-613.
    • (2001) Glycoconj J , vol.18 , pp. 589-613
    • Rudiger, H.1    Gabius, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.