메뉴 건너뛰기




Volumn 434, Issue 1, 2013, Pages 48-53

Structural insights into the coordination of iron by Thermus thermophilus HB8 ferric binding protein A

Author keywords

Conformation change; Ferric binding protein A; Thermus thermophilus HB8

Indexed keywords

CARBONIC ACID; FERRIC BINDING PROTEIN A; FERRIC ION; IRON BINDING PROTEIN; PERIPLASMIC BINDING PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84876806026     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.03.068     Document Type: Article
Times cited : (4)

References (29)
  • 1
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun V., Killmann H. Bacterial solutions to the iron-supply problem. Trends Biochem. Sci. 1999, 24:104-109.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 2
    • 0021356806 scopus 로고
    • Iron withholding: a defense against infection and neoplasia
    • Weinberg E.D. Iron withholding: a defense against infection and neoplasia. Physiol. Rev. 1984, 64:65-102.
    • (1984) Physiol. Rev. , vol.64 , pp. 65-102
    • Weinberg, E.D.1
  • 3
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman C., Delepelaire P. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 2004, 58:611-647.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 4
    • 0028850367 scopus 로고
    • Siderophores: structure and function of microbial iron transport compounds
    • Neilands J.B. Siderophores: structure and function of microbial iron transport compounds. J. Biol. Chem. 1995, 270:26723-26726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 5
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen S.D., Schryvers A.B. Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 1996, 4:185-191.
    • (1996) Trends Microbiol. , vol.4 , pp. 185-191
    • Gray-Owen, S.D.1    Schryvers, A.B.2
  • 7
    • 0343395846 scopus 로고    scopus 로고
    • ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
    • Koster W. ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12. Res. Microbiol. 2001, 152:291-301.
    • (2001) Res. Microbiol. , vol.152 , pp. 291-301
    • Koster, W.1
  • 9
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8A resolution
    • Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8A resolution. J. Mol. Biol. 1989, 209:711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 12
    • 15744377427 scopus 로고    scopus 로고
    • Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein
    • Tom-Yew S.A., Cui D.T., Bekker E.G., Murphy M.E. Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein. J. Biol. Chem. 2005, 280:9283-9290.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9283-9290
    • Tom-Yew, S.A.1    Cui, D.T.2    Bekker, E.G.3    Murphy, M.E.4
  • 14
    • 0037837866 scopus 로고    scopus 로고
    • High resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzae
    • Shouldice S.R., Dougan D.R., Skene R.J., Tari L.W., McRee D.E., Yu R.H., Schryvers A.B. High resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzae. J. Biol. Chem. 2003, 278:11513-11519.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11513-11519
    • Shouldice, S.R.1    Dougan, D.R.2    Skene, R.J.3    Tari, L.W.4    McRee, D.E.5    Yu, R.H.6    Schryvers, A.B.7
  • 15
    • 2942519288 scopus 로고    scopus 로고
    • Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens
    • Shouldice S.R., Skene R.J., Dougan D.R., Snell G., McRee D.E., Schryvers A.B., Tari L.W. Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens. J. Bacteriol. 2004, 186:3903-3910.
    • (2004) J. Bacteriol. , vol.186 , pp. 3903-3910
    • Shouldice, S.R.1    Skene, R.J.2    Dougan, D.R.3    Snell, G.4    McRee, D.E.5    Schryvers, A.B.6    Tari, L.W.7
  • 16
    • 14044274399 scopus 로고    scopus 로고
    • Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins
    • Shouldice S.R., McRee D.E., Dougan D.R., Tari L.W., Schryvers A.B. Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins. J. Biol. Chem. 2005, 280:5820-5827.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5820-5827
    • Shouldice, S.R.1    McRee, D.E.2    Dougan, D.R.3    Tari, L.W.4    Schryvers, A.B.5
  • 19
    • 79958089309 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary X-ray analysis of a ferric binding protein from Thermus thermophilus HB8
    • Wang Q., Chang L., Wang X., Liu X. Expression, crystallization and preliminary X-ray analysis of a ferric binding protein from Thermus thermophilus HB8. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2011, 67:723-726.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 723-726
    • Wang, Q.1    Chang, L.2    Wang, X.3    Liu, X.4
  • 20
    • 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. Macromol. Crystallogr., Pt A 1997, 276:307-326.
    • (1997) Macromol. Crystallogr., Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0013054388 scopus 로고    scopus 로고
    • Macromolecular phasing with SHELXE
    • Gm S. Macromolecular phasing with SHELXE. Z. Kristallogr. 2002, 217:644-650.
    • (2002) Z. Kristallogr. , vol.217 , pp. 644-650
    • Gm, S.1
  • 23
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs
    • Pape T., Schneider T.R. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J. Appl. Cryst. 2004, 37:843-844.
    • (2004) J. Appl. Cryst. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 24
    • 0028103275 scopus 로고
    • N. 4, The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project N. 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 1993, 26:283-291.
    • (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.