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Volumn 168, Issue 3, 2009, Pages 575-581

Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8

Author keywords

Alternative menaquinone biosynthetic pathway; DUF191; Menaquinone; MqnD; Thermus thermophilus

Indexed keywords

ASPARAGINE; ASPARTIC ACID; BACTERIAL ENZYME; GLUTAMIC ACID; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; MENAQUINONE; PROTEIN MQND; SERINE; TARTARIC ACID; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 70350383094     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.07.007     Document Type: Article
Times cited : (12)

References (23)
  • 4
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 5
    • 0036014793 scopus 로고    scopus 로고
    • Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium
    • Harding M.M. Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium. Acta Crystallogr. D 58 (2002) 872-874
    • (2002) Acta Crystallogr. D , vol.58 , pp. 872-874
    • Harding, M.M.1
  • 6
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254 (1991) 51-58
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 8
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 9
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 10
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 12
    • 33745615124 scopus 로고    scopus 로고
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity
    • Koropatkin N.M., Pakrasi H.B., and Smith T.J. Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity. Proc. Natl. Acad. Sci. USA 103 (2006) 9820-9825
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9820-9825
    • Koropatkin, N.M.1    Pakrasi, H.B.2    Smith, T.J.3
  • 14
  • 15
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 18
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallogr. D 58 (2002) 1937-1940
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 19
  • 21
    • 37749015568 scopus 로고    scopus 로고
    • X-ray structures of two proteins belonging to Pfam DUF178 revealed unexpected structural similarity to the DUF191 Pfam family
    • Tyagi R., Burley S.K., and Swaminathan S. X-ray structures of two proteins belonging to Pfam DUF178 revealed unexpected structural similarity to the DUF191 Pfam family. BMC Struct. Biol. 7 (2007) 62
    • (2007) BMC Struct. Biol. , vol.7 , pp. 62
    • Tyagi, R.1    Burley, S.K.2    Swaminathan, S.3
  • 23
    • 33644872571 scopus 로고    scopus 로고
    • LAFIRE: software for automating the refinement process of protein-structure analysis
    • Yao M., Zhou Y., and Tanaka I. LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Crystallogr. D 62 (2006) 189-196
    • (2006) Acta Crystallogr. D , vol.62 , pp. 189-196
    • Yao, M.1    Zhou, Y.2    Tanaka, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.