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Volumn 7, Issue , 2007, Pages

X-ray structures of two proteins belonging to Pfam DUF178 revealed unexpected structural similarity to the DUF191 Pfam family

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; DEINOCOCCUS RADIODURANS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN STRUCTURE; STREPTOMYCES COELICOLOR; X RAY ANALYSIS; BINDING SITE; CHEMISTRY; CLASSIFICATION; DEINOCOCCUS; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

EID: 37749015568     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-7-62     Document Type: Article
Times cited : (5)

References (20)
  • 3
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: Summaries and analyses of PDB structures.
    • 11125097. 10.1093/nar/29.1.221
    • PDBsum: summaries and analyses of PDB structures. RA Laskowski, Nucleic Acids Res 2001 29 221 222 11125097 10.1093/nar/29.1.221
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 4
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions.
    • 8552589. 10.1073/pnas.93.1.13
    • Principles of protein-protein interactions. S Jones JM Thornton, Proc Natl Acad Sci U S A 1996 93 13 20 8552589 10.1073/pnas.93.1.13
    • (1996) Proc Natl Acad Sci U S a , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 5
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices.
    • 10.1006/jmbi.1993.1489. 8377180
    • Protein structure comparison by alignment of distance matrices. L Holm C Sander, J Mol Biol 1993 233 123 138 10.1006/jmbi.1993.1489 8377180
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 8
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed Atlas of Surface Topography of proteins.
    • 12824325. 10.1093/nar/gkg512
    • CASTp: Computed Atlas of Surface Topography of proteins. TA Binkowski S Naghibzadeh J Liang, Nucleic Acids Research 2003 31 3352 3355 12824325 10.1093/nar/gkg512
    • (2003) Nucleic Acids Research , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 9
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.
    • 7984417. 10.1093/nar/22.22.4673
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. JD Thompson DG Higgins TJ Gibson, Nucleic Acids Res 1994 22 4673 4680 7984417 10.1093/nar/22.22.4673
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 11
    • 33745615124 scopus 로고    scopus 로고
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity.
    • 16777960. 10.1073/pnas.0602517103
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity. NM Koropatkin HB Pakrasi TJ Smith, Proc Natl Acad Sci U S A 103 9820 9825 16777960 10.1073/pnas.0602517103
    • Proc Natl Acad Sci U S a , vol.103 , pp. 9820-9825
    • Koropatkin, N.M.1    Pakrasi, H.B.2    Smith, T.J.3
  • 13
    • 33748999802 scopus 로고    scopus 로고
    • Crystal Structure of Glycerophosphodiester Phosphodiesterase from Agrobacterium tumefaciens by SAD with a Large Asymmetric Unit
    • 10.1002/prot.21079
    • Crystal Structure of Glycerophosphodiester Phosphodiesterase From Agrobacterium tumefaciens by SAD With a Large Asymmetric Unit. KN Rao JB Bonanno SK Burley S Swaminathan, Proteins: Structure, function, and Bioinformatics 2006 65 514 518 10.1002/prot.21079
    • (2006) Proteins: Structure, Function, and Bioinformatics , vol.65 , pp. 514-518
    • Rao, K.N.1    Bonanno, J.B.2    Burley, S.K.3    Swaminathan, S.4
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • "processing of X-ray Diffraction Data Collected in Oscillation Mode".
    • "Processing of X-ray Diffraction Data Collected in Oscillation Mode". Z Otwinowski W Minor, Methods Enzymol 1997 276 307 326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 15
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography.
    • 10.1016/S0959-440X(99)00020-2
    • Advances in direct methods for protein crystallography. I Uson GM Sheldrick, Curr Op Struct Biol 1999 9 643 648 10.1016/S0959-440X(99)00020-2
    • (1999) Curr Op Struct Biol , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 16
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods.
    • Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods. EDL Fortelle G Bricogne, Methods Enzymol 1997 276 472 493
    • (1997) Methods Enzymol , vol.276 , pp. 472-493
    • Fortelle, E.D.L.1    Bricogne, G.2
  • 17
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined iterative structure refinement.
    • 10.1038/8263. 10331874
    • Automated protein model building combined iterative structure refinement. A Perrakis R Morris VS Lamzin, Nat Struct Biol 1999 6 458 463 10.1038/8263 10331874
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models.
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models. TA Jones JY Zou SW Cowan M Kjeldgaard, Acta Crystallogr 1991 A47 110 119
    • (1991) Acta Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures.
    • 10.1107/S0021889892009944
    • PRO-CHECK: a program to check the stereochemical quality of protein structures. RA Laskowski MW MacArthur DS Moss JM Thornton, J Appl Cryst 1993 26 283 291 10.1107/S0021889892009944
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.