PDBsum entry 1g6h

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Transport protein PDB id
Protein chain
254 a.a. *
Waters ×406
* Residue conservation analysis
PDB id:
Name: Transport protein
Title: Crystal structure of the adp conformation of mj1267, an atp- binding cassette of an abc transporter
Structure: High-affinity branched-chain amino acid transport atp-binding protein. Chain: a
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190
Biol. unit: Dimer (from PQS)
1.60Å     R-factor:   0.217     R-free:   0.252
Authors: Y.-R.Yuan,O.Martsinkevich,N.Karpowich,L.Millen,P.J.Thomas, J.F.Hunt
Key ref:
N.Karpowich et al. (2001). Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure, 9, 571-586. PubMed id: 11470432 DOI: 10.1016/S0969-2126(01)00617-7
06-Nov-00     Release date:   18-Jul-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q58663  (LIVG_METJA) -  Probable branched-chain amino acid transport ATP-binding protein LivG
257 a.a.
254 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     nucleotide binding     3 terms  


DOI no: 10.1016/S0969-2126(01)00617-7 Structure 9:571-586 (2001)
PubMed id: 11470432  
Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter.
N.Karpowich, O.Martsinkevich, L.Millen, Y.R.Yuan, P.L.Dai, K.MacVey, P.J.Thomas, J.F.Hunt.
BACKGROUND: ATP binding cassette (ABC) transporters are ubiquitously distributed transmembrane solute pumps that play a causative role in numerous diseases. Previous structures have defined the fold of the ABC and established the flexibility of its alpha-helical subdomain. But the nature of the mechanical changes that occur at each step of the chemical ATPase cycle have not been defined. RESULTS: Crystal structures were determined of the MJ1267 ABC from Methanococcus jannaschii in Mg-ADP-bound and nucleotide-free forms. Comparison of these structures reveals an induced-fit effect at the active site likely to be a consequence of nucleotide binding. In the Mg-ADP-bound structure, the loop following the Walker B moves toward the Walker A (P-loop) coupled to backbone conformational changes in the intervening "H-loop", which contains an invariant histidine. These changes affect the region believed to mediate intercassette interaction in the ABC transporter complex. Comparison of the Mg-ADP-bound structure of MJ1267 to the ATP-bound structure of HisP suggests that an outward rotation of the alpha-helical subdomain is coupled to the loss of a molecular contact between the gamma-phosphate of ATP and an invariant glutamine in a segment connecting this subdomain to the core of the cassette. CONCLUSIONS: The induced-fit effect and rotation of the alpha-helical subdomain may play a role in controlling the nucleotide-dependent change in cassette-cassette interaction affinity believed to represent the power-stroke of ABC transporters. Outward rotation of the alpha-helical subdomain also likely facilitates Mg-ADP release after hydrolysis. The MJ1267 structures therefore define features of the nucleotide-dependent conformational changes that drive transmembrane transport in ABC transporters.
  Selected figure(s)  
Figure 4.
Figure 4. Cooperative Structural Interactions Involving Phylogenetically Conserved Residues Stabilize Limiting Conformations of the g-Phosphate LinkerH bonds in the g-phosphate linker region identified based on having a heteroatom separation =< 3.4 are represented by dotted orange lines in the stereo pairs [57 and 58] showing:(a) The ATP-bound structure of HisP [16].(b) The Mg-ADP-bound structure of MJ0796 [21].(c) The Mg-ADP-bound structure of MJ1267.(d) One of the two NCS-related molecules in the pyrophosphate-bound structure of MalK [17].Residues with side chains participating in alternative H bonding networks with phylogenetically conserved Arg166 are shown in cyan. Relative to MJ1267, homologous residues in the g-phosphate linker region are offset by +1 in MJ0796, +11 in HisP, and -1 in MalK, and homologous residues in the C terminus of the ABCa subdomain are offset by -8 in MJ0796, +0 in HisP, and -14 in MalK

  The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 571-586) copyright 2001.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21488101 A.S.Oliveira, A.M.Baptista, and C.M.Soares (2011).
Conformational changes induced by ATP-hydrolysis in an ABC transporter: A molecular dynamics study of the Sav1866 exporter.
  Proteins, 79, 1977-1990.  
21194365 R.P.Gupta, P.Kueppers, L.Schmitt, and R.Ernst (2011).
The multidrug transporter Pdr5: a molecular diode?
  Biol Chem, 392, 53-60.  
21315686 R.Yang, Y.X.Hou, C.A.Campbell, K.Palaniyandi, Q.Zhao, A.J.Bordner, and X.B.Chang (2011).
Glutamine residues in Q-loops of multidrug resistance protein MRP1 contribute to ATP binding via interaction with metal cofactor.
  Biochim Biophys Acta, 1808, 1790-1796.  
20497229 T.Eitinger, D.A.Rodionov, M.Grote, and E.Schneider (2011).
Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
  FEMS Microbiol Rev, 35, 3.  
20687163 C.Wang, I.Protasevich, Z.Yang, D.Seehausen, T.Skalak, X.Zhao, S.Atwell, J.Spencer Emtage, D.R.Wetmore, C.G.Brouillette, and J.F.Hunt (2010).
Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.
  Protein Sci, 19, 1932-1947.  
  20421370 M.F.Tsai, M.Li, and T.C.Hwang (2010).
Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel.
  J Gen Physiol, 135, 399-414.  
20823549 M.Haffke, A.Menzel, Y.Carius, D.Jahn, and D.W.Heinz (2010).
Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.
  Acta Crystallogr D Biol Crystallogr, 66, 979-987.
PDB codes: 3nh6 3nh9 3nha 3nhb
20110677 M.Kloch, M.Milewski, E.Nurowska, B.Dworakowska, G.R.Cutting, and K.Dołowy (2010).
The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing.
  Cell Physiol Biochem, 25, 169-180.  
19234479 D.C.Rees, E.Johnson, and O.Lewinson (2009).
ABC transporters: the power to change.
  Nat Rev Mol Cell Biol, 10, 218-227.  
19250913 D.Khare, M.L.Oldham, C.Orelle, A.L.Davidson, and J.Chen (2009).
Alternating access in maltose transporter mediated by rigid-body rotations.
  Mol Cell, 33, 528-536.
PDB code: 3fh6
18957373 D.Muallem, and P.Vergani (2009).
Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator.
  Philos Trans R Soc Lond B Biol Sci, 364, 247-255.  
19368888 J.Timmins, E.Gordon, S.Caria, G.Leonard, S.Acajjaoui, M.S.Kuo, V.Monchois, and S.McSweeney (2009).
Structural and mutational analyses of Deinococcus radiodurans UvrA2 provide insight into DNA binding and damage recognition by UvrAs.
  Structure, 17, 547-558.
PDB codes: 2vf7 2vf8
18831048 P.M.Jones, and A.M.George (2009).
Opening of the ADP-bound active site in the ABC transporter ATPase dimer: evidence for a constant contact, alternating sites model for the catalytic cycle.
  Proteins, 75, 387-396.  
19748784 P.M.Jones, M.L.O'Mara, and A.M.George (2009).
ABC transporters: a riddle wrapped in a mystery inside an enigma.
  Trends Biochem Sci, 34, 520-531.  
19265398 S.Balaz (2009).
Modeling kinetics of subcellular disposition of chemicals.
  Chem Rev, 109, 1793-1899.  
19748342 S.Newstead, P.W.Fowler, P.Bilton, E.P.Carpenter, P.J.Sadler, D.J.Campopiano, M.S.Sansom, and S.Iwata (2009).
Insights into how nucleotide-binding domains power ABC transport.
  Structure, 17, 1213-1222.
PDB code: 3fvq
19453273 U.A.Hellmich, and C.Glaubitz (2009).
NMR and EPR studies of membrane transporters.
  Biol Chem, 390, 815-834.  
19691360 Y.X.Hou, C.Z.Li, K.Palaniyandi, P.M.Magtibay, L.Homolya, B.Sarkadi, and X.B.Chang (2009).
Effects of putative catalytic base mutation E211Q on ABCG2-mediated methotrexate transport.
  Biochemistry, 48, 9122-9131.  
18158267 D.Pakotiprapha, Y.Inuzuka, B.R.Bowman, G.F.Moolenaar, N.Goosen, D.Jeruzalmi, and G.L.Verdine (2008).
Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding.
  Mol Cell, 29, 122-133.
PDB code: 2r6f
18057957 H.Schillers (2008).
Imaging CFTR in its native environment.
  Pflugers Arch, 456, 163-177.  
18304008 J.R.Riordan (2008).
CFTR function and prospects for therapy.
  Annu Rev Biochem, 77, 701-726.  
17951296 J.Weng, J.Ma, K.Fan, and W.Wang (2008).
The conformational coupling and translocation mechanism of vitamin B12 ATP-binding cassette transporter BtuCD.
  Biophys J, 94, 612-621.  
18235435 N.E.Chayen, and E.Saridakis (2008).
Protein crystallization: from purified protein to diffraction-quality crystal.
  Nat Methods, 5, 147-153.  
17208306 C.A.McDevitt, and R.Callaghan (2007).
How can we best use structural information on P-glycoprotein to design inhibitors?
  Pharmacol Ther, 113, 429-441.  
18078545 C.D.Putnam, M.Hammel, G.L.Hura, and J.A.Tainer (2007).
X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution.
  Q Rev Biophys, 40, 191-285.  
17158291 H.W.Pinkett, A.T.Lee, P.Lum, K.P.Locher, and D.C.Rees (2007).
An inward-facing conformation of a putative metal-chelate-type ABC transporter.
  Science, 315, 373-377.
PDB code: 2nq2
17804665 M.Miethke, and M.A.Marahiel (2007).
Siderophore-based iron acquisition and pathogen control.
  Microbiol Mol Biol Rev, 71, 413-451.  
17485460 P.M.Jones, and A.M.George (2007).
Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: a computational study of the MJ0796 dimer.
  J Biol Chem, 282, 22793-22803.  
17764951 S.J.Lee, A.Böhm, M.Krug, and W.Boos (2007).
The ABC of binding-protein-dependent transport in Archaea.
  Trends Microbiol, 15, 389-397.  
17029409 A.H.Buchaklian, and C.S.Klug (2006).
Characterization of the LSGGQ and H motifs from the Escherichia coli lipid A transporter MsbA.
  Biochemistry, 45, 12539-12546.  
16541253 C.Oswald, I.B.Holland, and L.Schmitt (2006).
The motor domains of ABC-transporters. What can structures tell us?
  Naunyn Schmiedebergs Arch Pharmacol, 372, 385-399.  
16783375 D.Keramisanou, N.Biris, I.Gelis, G.Sianidis, S.Karamanou, A.Economou, and C.G.Kalodimos (2006).
Disorder-order folding transitions underlie catalysis in the helicase motor of SecA.
  Nat Struct Mol Biol, 13, 594-602.  
16407313 D.Murat, P.Bance, I.Callebaut, and E.Dassa (2006).
ATP hydrolysis is essential for the function of the Uup ATP-binding cassette ATPase in precise excision of transposons.
  J Biol Chem, 281, 6850-6859.  
17215877 E.O.Oloo, C.Kandt, M.L.O'Mara, and D.P.Tieleman (2006).
Computer simulations of ABC transporter components.
  Biochem Cell Biol, 84, 900-911.  
17018292 E.Procko, I.Ferrin-O'Connell, S.L.Ng, and R.Gaudet (2006).
Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter.
  Mol Cell, 24, 51-62.
PDB codes: 2ixe 2ixf 2ixg
16858415 J.Zaitseva, C.Oswald, T.Jumpertz, S.Jenewein, A.Wiedenmann, I.B.Holland, and L.Schmitt (2006).
A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.
  EMBO J, 25, 3432-3443.
PDB codes: 2ff7 2ffa 2ffb 2fgj 2fgk
16791740 K.Kurashima-Ito, T.Ikeya, H.Senbongi, H.Tochio, T.Mikawa, T.Shibata, and Y.Ito (2006).
Heteronuclear multidimensional NMR and homology modelling studies of the C-terminal nucleotide-binding domain of the human mitochondrial ABC transporter ABCB6.
  J Biomol NMR, 35, 53-71.  
17036051 M.Mense, P.Vergani, D.M.White, G.Altberg, A.C.Nairn, and D.C.Gadsby (2006).
In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.
  EMBO J, 25, 4728-4739.  
16547024 X.Guo, R.W.Harrison, and P.C.Tai (2006).
Nucleotide-dependent dimerization of the C-terminal domain of the ABC transporter CvaB in colicin V secretion.
  J Bacteriol, 188, 2383-2391.  
17128986 X.Guo, X.Chen, I.T.Weber, R.W.Harrison, and P.C.Tai (2006).
Molecular basis for differential nucleotide binding of the nucleotide-binding domain of ABC-transporter CvaB.
  Biochemistry, 45, 14473-14480.  
  16966475 Z.Zhou, X.Wang, H.Y.Liu, X.Zou, M.Li, and T.C.Hwang (2006).
The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.
  J Gen Physiol, 128, 413-422.  
15837203 A.Karcher, K.Büttner, B.Märtens, R.P.Jansen, and K.P.Hopfner (2005).
X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly.
  Structure, 13, 649-659.
PDB code: 1yqt
16691491 C.Schölz, and R.Tampé (2005).
The intracellular antigen transport machinery TAP in adaptive immunity and virus escape mechanisms.
  J Bioenerg Biomembr, 37, 509-515.  
16691486 J.E.Moody, and P.J.Thomas (2005).
Nucleotide binding domain interactions during the mechanochemical reaction cycle of ATP-binding cassette transporters.
  J Bioenerg Biomembr, 37, 475-479.  
15709975 J.R.Riordan (2005).
Assembly of functional CFTR chloride channels.
  Annu Rev Physiol, 67, 701-718.  
15889153 J.Zaitseva, S.Jenewein, T.Jumpertz, I.B.Holland, and L.Schmitt (2005).
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB.
  EMBO J, 24, 1901-1910.
PDB code: 1xef
  15596536 L.Csanády, K.W.Chan, A.C.Nairn, and D.C.Gadsby (2005).
Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain.
  J Gen Physiol, 125, 43-55.  
15619636 P.H.Thibodeau, C.A.Brautigam, M.Machius, and P.J.Thomas (2005).
Side chain and backbone contributions of Phe508 to CFTR folding.
  Nat Struct Mol Biol, 12, 10-16.
PDB codes: 1xf9 1xfa
16246032 P.Vergani, C.Basso, M.Mense, A.C.Nairn, and D.C.Gadsby (2005).
Control of the CFTR channel's gates.
  Biochem Soc Trans, 33, 1003-1007.  
  15767296 S.G.Bompadre, J.H.Cho, X.Wang, X.Zou, Y.Sohma, M.Li, and T.C.Hwang (2005).
CFTR gating II: Effects of nucleotide binding on the stability of open states.
  J Gen Physiol, 125, 377-394.  
16456713 T.W.Loo, and D.M.Clarke (2005).
Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux.
  J Membr Biol, 206, 173-185.  
15189142 A.L.Davidson, and J.Chen (2004).
ATP-binding cassette transporters in bacteria.
  Annu Rev Biochem, 73, 241-268.  
15551867 C.van der Does, and R.Tampé (2004).
How do ABC transporters drive transport?
  Biol Chem, 385, 927-933.  
15308647 E.O.Oloo, and D.P.Tieleman (2004).
Conformational transitions induced by the binding of MgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD.
  J Biol Chem, 279, 45013-45019.  
14685259 H.A.Lewis, S.G.Buchanan, S.K.Burley, K.Conners, M.Dickey, M.Dorwart, R.Fowler, X.Gao, W.B.Guggino, W.A.Hendrickson, J.F.Hunt, M.C.Kearins, D.Lorimer, P.C.Maloney, K.W.Post, K.R.Rajashankar, M.E.Rutter, J.M.Sauder, S.Shriver, P.H.Thibodeau, P.J.Thomas, M.Zhang, X.Zhao, and S.Emtage (2004).
Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator.
  EMBO J, 23, 282-293.
PDB codes: 1q3h 1r0w 1r0x 1r0y 1r0z 1r10
15377525 J.D.Campbell, S.S.Deol, F.M.Ashcroft, I.D.Kerr, and M.S.Sansom (2004).
Nucleotide-dependent conformational changes in HisP: molecular dynamics simulations of an ABC transporter nucleotide-binding domain.
  Biophys J, 87, 3703-3715.  
15159567 J.Zaitseva, I.B.Holland, and L.Schmitt (2004).
The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 60, 1076-1084.  
15313236 K.P.Locher (2004).
Structure and mechanism of ABC transporters.
  Curr Opin Struct Biol, 14, 426-431.  
  15520867 R.Frikke-Schmidt, B.G.Nordestgaard, G.B.Jensen, and A.Tybjaerg-Hansen (2004).
Genetic variation in ABC transporter A1 contributes to HDL cholesterol in the general population.
  J Clin Invest, 114, 1343-1353.  
  12939393 C.Basso, P.Vergani, A.C.Nairn, and D.C.Gadsby (2003).
Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.
  J Gen Physiol, 122, 333-348.  
14697202 C.Randak, and M.J.Welsh (2003).
An intrinsic adenylate kinase activity regulates gating of the ABC transporter CFTR.
  Cell, 115, 837-850.  
12496311 E.A.Cartier, S.Shen, and S.L.Shyng (2003).
Modulation of the trafficking efficiency and functional properties of ATP-sensitive potassium channels through a single amino acid in the sulfonylurea receptor.
  J Biol Chem, 278, 7081-7090.  
12746444 E.Janas, M.Hofacker, M.Chen, S.Gompf, C.van der Does, and R.Tampé (2003).
The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p.
  J Biol Chem, 278, 26862-26869.  
12654004 G.Berridge, J.A.Walker, R.Callaghan, and I.D.Kerr (2003).
The nucleotide-binding domains of P-glycoprotein. Functional symmetry in the isolated domain demonstrated by N-ethylmaleimide labelling.
  Eur J Biochem, 270, 1483-1492.  
12830334 I.D.Kerr, G.Berridge, K.J.Linton, C.F.Higgins, and R.Callaghan (2003).
Definition of the domain boundaries is critical to the expression of the nucleotide-binding domains of P-glycoprotein.
  Eur Biophys J, 32, 644-654.  
14527411 J.Chen, G.Lu, J.Lin, A.L.Davidson, and F.A.Quiocho (2003).
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle.
  Mol Cell, 12, 651-661.
PDB codes: 1q12 1q1b 1q1e
14593442 J.D.Campbell, M.S.Sansom, and F.M.Ashcroft (2003).
Potassium channel regulation.
  EMBO Rep, 4, 1038-1042.  
12667056 J.D.Campbell, P.C.Biggin, M.Baaden, and M.S.Sansom (2003).
Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA.
  Biochemistry, 42, 3666-3673.  
12526851 K.S.McKeegan, M.I.Borges-Walmsley, and A.R.Walmsley (2003).
The structure and function of drug pumps: an update.
  Trends Microbiol, 11, 21-29.  
  12508051 P.Vergani, A.C.Nairn, and D.C.Gadsby (2003).
On the mechanism of MgATP-dependent gating of CFTR Cl- channels.
  J Gen Physiol, 121, 17-36.  
12813052 S.Samanta, T.Ayvaz, M.Reyes, H.A.Shuman, J.Chen, and A.L.Davidson (2003).
Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex.
  J Biol Chem, 278, 35265-35271.  
12554933 Y.R.Yuan, O.Martsinkevich, and J.F.Hunt (2003).
Structural characterization of an MJ1267 ATP-binding cassette crystal with a complex pattern of twinning caused by promiscuous fiber packing.
  Acta Crystallogr D Biol Crystallogr, 59, 225-238.
PDB code: 1g9x
11844750 A.L.Davidson (2002).
Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters.
  J Bacteriol, 184, 1225-1233.  
12180984 A.Stein, M.Seifert, R.Volkmer-Engert, J.Siepelmeyer, K.Jahreis, and E.Schneider (2002).
Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit.
  Eur J Biochem, 269, 4074-4085.  
11964392 J.E.Moody, L.Millen, D.Binns, J.F.Hunt, and P.J.Thomas (2002).
Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters.
  J Biol Chem, 277, 21111-21114.  
12163504 J.Y.Lee, I.L.Urbatsch, A.E.Senior, and S.Wilkens (2002).
Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains.
  J Biol Chem, 277, 40125-40131.  
11856849 L.Kránitz, H.Benabdelhak, C.Horn, M.A.Blight, I.B.Holland, and L.Schmitt (2002).
Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli.
  Acta Crystallogr D Biol Crystallogr, 58, 539-541.  
11825892 L.V.Zingman, D.M.Hodgson, M.Bienengraeber, A.B.Karger, E.C.Kathmann, A.E.Alekseev, and A.Terzic (2002).
Tandem function of nucleotide binding domains confers competence to sulfonylurea receptor in gating ATP-sensitive K+ channels.
  J Biol Chem, 277, 14206-14210.  
12150914 P.C.Smith, N.Karpowich, L.Millen, J.E.Moody, J.Rosen, P.J.Thomas, and J.F.Hunt (2002).
ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.
  Mol Cell, 10, 139-149.
PDB code: 1l2t
12209147 P.Chène (2002).
ATPases as drug targets: learning from their structure.
  Nat Rev Drug Discov, 1, 665-673.  
12237398 P.M.Jones, and A.M.George (2002).
Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit.
  Proc Natl Acad Sci U S A, 99, 12639-12644.  
12217520 P.M.van Endert, L.Saveanu, E.W.Hewitt, and P.Lehner (2002).
Powering the peptide pump: TAP crosstalk with energetic nucleotides.
  Trends Biochem Sci, 27, 454-461.  
12070134 T.W.Loo, M.C.Bartlett, and D.M.Clarke (2002).
Introduction of the most common cystic fibrosis mutation (Delta F508) into human P-glycoprotein disrupts packing of the transmembrane segments.
  J Biol Chem, 277, 27585-27588.  
11589692 A.Sharff, C.Fanutti, J.Shi, C.Calladine, and B.Luisi (2001).
The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis.
  Eur J Biochem, 268, 5011-5026.  
11595746 G.Velarde, R.C.Ford, M.F.Rosenberg, and S.J.Powis (2001).
Three-dimensional structure of transporter associated with antigen processing (TAP) obtained by single Particle image analysis.
  J Biol Chem, 276, 46054-46063.  
11685233 P.J.Thomas, and J.F.Hunt (2001).
A snapshot of Nature's favorite pump.
  Nat Struct Biol, 8, 920-923.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.