메뉴 건너뛰기




Volumn 392, Issue 3, 2009, Pages 559-565

Crystal Structure of a Periplasmic Substrate-Binding Protein in Complex with Calcium Lactate

Author keywords

calcium; crystal structure; lactate; periplasmic substrate binding protein; TRAP transporter

Indexed keywords

CALCIUM ION; CALCIUM LACTATE; LACTIC ACID; PERIPLASMIC BINDING PROTEIN; TRIPARTITE ADENOSINE TRIPHOSPHATE INDEPENDENT PERIPLASMIC TRANSPORTER; UNCLASSIFIED DRUG;

EID: 69349104451     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.043     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0030967906 scopus 로고    scopus 로고
    • TRAP transporters: a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria
    • Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., and Kelly D.J. TRAP transporters: a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria. J. Bacteriol. 179 (1997) 5482-5493
    • (1997) J. Bacteriol. , vol.179 , pp. 5482-5493
    • Forward, J.A.1    Behrendt, M.C.2    Wyborn, N.R.3    Cross, R.4    Kelly, D.J.5
  • 2
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly D.J., and Thomas G.H. The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea. FEMS Microbiol. Rev. 25 (2001) 405-424
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 405-424
    • Kelly, D.J.1    Thomas, G.H.2
  • 3
    • 0033374883 scopus 로고    scopus 로고
    • TRAP transporters: an ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters
    • Rabus R., Jack D.L., Kelly D.J., and Saier Jr. M.H. TRAP transporters: an ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters. Microbiology 145 (1999) 3431-3445
    • (1999) Microbiology , vol.145 , pp. 3431-3445
    • Rabus, R.1    Jack, D.L.2    Kelly, D.J.3    Saier Jr., M.H.4
  • 4
    • 0003688859 scopus 로고    scopus 로고
    • Prokaryotic binding protein-dependent ABC transporters
    • Winkelmann G. (Ed), Wiley-VCH, Weinheim, Germany
    • Boos W., and Eppler T. Prokaryotic binding protein-dependent ABC transporters. In: Winkelmann G. (Ed). Microbial Transport Systems (2001), Wiley-VCH, Weinheim, Germany 77-114
    • (2001) Microbial Transport Systems , pp. 77-114
    • Boos, W.1    Eppler, T.2
  • 5
    • 31344463251 scopus 로고    scopus 로고
    • Crystal structure of Bordetella pertussis BugD solute receptor unveils the basis of ligand binding in a new family of periplasmic binding proteins
    • Huvent I., Belrhali H., Antoine R., Bompard C., Locht C., Jacob-Dubuisson F., and Villeret V. Crystal structure of Bordetella pertussis BugD solute receptor unveils the basis of ligand binding in a new family of periplasmic binding proteins. J. Mol. Biol. 356 (2006) 1014-1026
    • (2006) J. Mol. Biol. , vol.356 , pp. 1014-1026
    • Huvent, I.1    Belrhali, H.2    Antoine, R.3    Bompard, C.4    Locht, C.5    Jacob-Dubuisson, F.6    Villeret, V.7
  • 6
    • 33746848092 scopus 로고    scopus 로고
    • Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae
    • Muller A., Severi E., Mulligan C., Watts A.G., Kelly D.J., Wilson K.S., et al. Conservation of structure and mechanism in primary and secondary transporters exemplified by SiaP, a sialic acid binding virulence factor from Haemophilus influenzae. J. Biol. Chem. 281 (2006) 22212-22222
    • (2006) J. Biol. Chem. , vol.281 , pp. 22212-22222
    • Muller, A.1    Severi, E.2    Mulligan, C.3    Watts, A.G.4    Kelly, D.J.5    Wilson, K.S.6
  • 7
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding
    • Gonin S., Arnoux P., Pierru B., Lavergne J., Alonso B., Sabaty M., and Pignol D. Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding. BMC Struct. Biol. 7 (2007) 11
    • (2007) BMC Struct. Biol. , vol.7 , pp. 11
    • Gonin, S.1    Arnoux, P.2    Pierru, B.3    Lavergne, J.4    Alonso, B.5    Sabaty, M.6    Pignol, D.7
  • 8
    • 34249288692 scopus 로고    scopus 로고
    • Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily
    • Rucktooa P., Antoine R., Herrou J., Huvent I., Locht C., Jacob-Dubuisson F., et al. Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily. J. Mol. Biol. 370 (2007) 93-106
    • (2007) J. Mol. Biol. , vol.370 , pp. 93-106
    • Rucktooa, P.1    Antoine, R.2    Herrou, J.3    Huvent, I.4    Locht, C.5    Jacob-Dubuisson, F.6
  • 9
    • 57749104100 scopus 로고    scopus 로고
    • Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport
    • Cuneo M.J., Changela A., Miklos A.E., Beese L.S., Krueger J.K., and Hellinga H.W. Structural analysis of a periplasmic binding protein in the tripartite ATP-independent transporter family reveals a tetrameric assembly that may have a role in ligand transport. J. Biol. Chem. 283 (2008) 32812-32820
    • (2008) J. Biol. Chem. , vol.283 , pp. 32812-32820
    • Cuneo, M.J.1    Changela, A.2    Miklos, A.E.3    Beese, L.S.4    Krueger, J.K.5    Hellinga, H.W.6
  • 10
    • 51649116054 scopus 로고    scopus 로고
    • 1.55 Å structure of the ectoine binding protein TeaA of the osmoregulated TRAP-transporter TeaABC from Halomonas elongata
    • Kuhlmann S.I., Terwisscha van Scheltinga A.C., Bienert R., Kunte H.J., and Ziegler C. 1.55 Å structure of the ectoine binding protein TeaA of the osmoregulated TRAP-transporter TeaABC from Halomonas elongata. Biochemistry 47 (2008) 9475-9485
    • (2008) Biochemistry , vol.47 , pp. 9475-9485
    • Kuhlmann, S.I.1    Terwisscha van Scheltinga, A.C.2    Bienert, R.3    Kunte, H.J.4    Ziegler, C.5
  • 11
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 12
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi K., Tateno Y., and Nishikawa K. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 286 (1999) 279-290
    • (1999) J. Mol. Biol. , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 13
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors
    • Felder C.B., Graul R.C., Lee A.Y., Merkle H.P., and Sadee W. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci. 1 (1999) E2
    • (1999) AAPS PharmSci. , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 14
    • 85008065603 scopus 로고
    • Isolation of an extreme thermophile and thermostability of its transfer ribonucleic acid and ribosomes
    • Oshima T., and Imahori K. Isolation of an extreme thermophile and thermostability of its transfer ribonucleic acid and ribosomes. J. Gen. Appl. Microbiol. 17 (1971) 513-517
    • (1971) J. Gen. Appl. Microbiol. , vol.17 , pp. 513-517
    • Oshima, T.1    Imahori, K.2
  • 15
    • 3242878999 scopus 로고    scopus 로고
    • PrediSi: prediction of signal peptides and their cleavage positions
    • Hiller K., Grote A., Scheer M., Munch R., and Jahn D. PrediSi: prediction of signal peptides and their cleavage positions. Nucleic Acids Res. 32 (2004) W375-379
    • (2004) Nucleic Acids Res. , vol.32
    • Hiller, K.1    Grote, A.2    Scheer, M.3    Munch, R.4    Jahn, D.5
  • 16
    • 59449110078 scopus 로고    scopus 로고
    • SOSUI-GramN: high performance prediction for subcellular localization of proteins in Gram-negative bacteria
    • Imai K., Asakawa N., Tsuji T., Akazawa F., Ino A., Sonoyama M., and Mitaku S. SOSUI-GramN: high performance prediction for subcellular localization of proteins in Gram-negative bacteria. Bioinformation 2 (2008) 417-421
    • (2008) Bioinformation , vol.2 , pp. 417-421
    • Imai, K.1    Asakawa, N.2    Tsuji, T.3    Akazawa, F.4    Ino, A.5    Sonoyama, M.6    Mitaku, S.7
  • 17
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP, and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP, and related tools. Nat. Protoc. 2 (2007) 953-971
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 18
    • 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
  • 21
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 22
    • 84889120137 scopus 로고
    • Improved methods for binding 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 binding 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
  • 24
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Thornton, J.M.3
  • 29
    • 0028871926 scopus 로고
    • DALI: a network tool for protein-structure comparison
    • Holm L., and Sander C. DALI: a network tool for protein-structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 30
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins
    • Harding M.M. The geometry of metal-ligand interactions relevant to proteins. Acta Crystallogr., Sect. D: Biol. Crystallogr. 55 (1999) 1432-1443
    • (1999) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 31
    • 0033569442 scopus 로고    scopus 로고
    • The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation
    • Halestrap A.P., and Price N.T. The proton-linked monocarboxylate transporter (MCT) family: structure, function and regulation. Biochem. J. 343 (1999) 281-299
    • (1999) Biochem. J. , vol.343 , pp. 281-299
    • Halestrap, A.P.1    Price, N.T.2
  • 32
    • 0036462412 scopus 로고    scopus 로고
    • Muscle fatigue: lactic acid or inorganic phosphate the major cause?
    • Westerblad H., Allen D.G., and Lannergren J. Muscle fatigue: lactic acid or inorganic phosphate the major cause?. News Physiol. Sci. 17 (2002) 17-21
    • (2002) News Physiol. Sci. , vol.17 , pp. 17-21
    • Westerblad, H.1    Allen, D.G.2    Lannergren, J.3
  • 33
    • 4344608324 scopus 로고    scopus 로고
    • Physiology. Lactic acid-the latest performance-enhancing drug
    • Allen D., and Westerblad H. Physiology. Lactic acid-the latest performance-enhancing drug. Science 305 (2004) 1112-1113
    • (2004) Science , vol.305 , pp. 1112-1113
    • Allen, D.1    Westerblad, H.2
  • 34
    • 60549098063 scopus 로고    scopus 로고
    • The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter
    • Mulligan C., Geertsma E.R., Severi E., Kelly D.J., Poolman B., and Thomas G.H. The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc. Natl Acad. Sci. USA 106 (2009) 1778-1783
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1778-1783
    • Mulligan, C.1    Geertsma, E.R.2    Severi, E.3    Kelly, D.J.4    Poolman, B.5    Thomas, G.H.6
  • 35
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham M.L., Khare D., Quiocho F.A., Davidson A.L., and Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 (2007) 515-521
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.