메뉴 건너뛰기




Volumn 63, Issue 4, 2006, Pages 733-741

Crystal structure of VC0702 at 2.0 Å: Conserved hypothetical protein from Vibrio cholerae

Author keywords

Biofilm regulation; dNTPase; dUTPase; MbaA; Pyrophosphatase; VC0702; VC0703; Vibrio cholerae

Indexed keywords

BACTERIAL PROTEIN; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; GENOMIC DNA; INORGANIC PYROPHOSPHATASE; UNCLASSIFIED DRUG; VC0702 PROTEIN;

EID: 33646762769     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20919     Document Type: Article
Times cited : (2)

References (16)
  • 2
    • 0037312852 scopus 로고    scopus 로고
    • Identification and characterization of a Vibrio cholerae gene, mbaA, involved in maintenance of biofilm architecture
    • Bomchil N, Watnick P, Kolter R. Identification and characterization of a Vibrio cholerae gene, mbaA, involved in maintenance of biofilm architecture. J Bacteriol 2003;185:1384-1390.
    • (2003) J Bacteriol , vol.185 , pp. 1384-1390
    • Bomchil, N.1    Watnick, P.2    Kolter, R.3
  • 3
    • 4444250897 scopus 로고    scopus 로고
    • Cyclic di-GMP as a bacterial second messenger
    • D'Argenio D, Miller SI. Cyclic di-GMP as a bacterial second messenger. Microbiology 2004;150:2497-2502.
    • (2004) Microbiology , vol.150 , pp. 2497-2502
    • D'Argenio, D.1    Miller, S.I.2
  • 4
    • 17444398048 scopus 로고    scopus 로고
    • Structure-based identification of a novel NTPase from Methanococcus jannaschii
    • Hwang KY, Chung JH, Kim SH, Han YS, Cho Y. Structure-based identification of a novel NTPase from Methanococcus jannaschii. Nat Struct Biol 1999;6:691-696.
    • (1999) Nat Struct Biol , vol.6 , pp. 691-696
    • Hwang, K.Y.1    Chung, J.H.2    Kim, S.H.3    Han, Y.S.4    Cho, Y.5
  • 5
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:207-326.
    • (1997) Methods Enzymol , vol.276 , pp. 207-326
    • Otwinowski, Z.1    Minor, W.2
  • 6
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger T, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D 1999;D55:849-861.
    • (1999) Acta Crystallogr D , vol.D55 , pp. 849-861
    • Terwilliger, T.1    Berendzen, J.2
  • 7
    • 0033229974 scopus 로고    scopus 로고
    • Reciprocal-space solvent flattening
    • Terwilliger T. Reciprocal-space solvent flattening. Acta Crystallogr D 1999;D55:1863-1871.
    • (1999) Acta Crystallogr D , vol.D55 , pp. 1863-1871
    • Terwilliger, T.1
  • 8
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T. Maximum-likelihood density modification. Acta Crystallogr D 2000;D56:965-972.
    • (2000) Acta Crystallogr D , vol.D56 , pp. 965-972
    • Terwilliger, T.1
  • 9
    • 0035210945 scopus 로고    scopus 로고
    • Maximum-likelihood density modification using pattern recognition of structural motifs
    • Terwilliger T. Maximum-likelihood density modification using pattern recognition of structural motifs. Acta Crystallogr D 2001; D57:1755-1762.
    • (2001) Acta Crystallogr D , vol.D57 , pp. 1755-1762
    • Terwilliger, T.1
  • 10
    • 0035207615 scopus 로고    scopus 로고
    • Map-likelihood phasing
    • Terwilliger T. Map-likelihood phasing. Acta Crystallogr D 2001; D57:1763-1775.
    • (2001) Acta Crystallogr D , vol.D57 , pp. 1763-1775
    • Terwilliger, T.1
  • 11
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee D. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 1999;125: 156-165.
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.1
  • 13
    • 0000243829 scopus 로고
    • PRO-CHECK - A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PRO-CHECK - a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 14
    • 0034612280 scopus 로고    scopus 로고
    • Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP
    • Minasov G, Teplova M, Stewart GC, Koonin EV, Anderson WF, Egli M. Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP. Proc Natl Acad Sci U S A 2000;97:6328-6333.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6328-6333
    • Minasov, G.1    Teplova, M.2    Stewart, G.C.3    Koonin, E.V.4    Anderson, W.F.5    Egli, M.6
  • 15
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 16
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.