Genome Research

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Arnesano, F.
Right arrow Articles by O'Halloran, T. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Arnesano, F.
Right arrow Articles by O'Halloran, T. V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Vol. 12, Issue 2, 255-271, February 2002

Metallochaperones and Metal-Transporting ATPases: A Comparative Analysis of Sequences and Structures

Fabio Arnesano,1 Lucia Banci,1 Ivano Bertini,1,3 Simone Ciofi-Baffoni,1 Elena Molteni,1 David L. Huffman,2 and Thomas V. O'Halloran2

1 Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy; 2 Department of Chemistry and the Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA

A comparative structural genomic analysis of a new class of metal-trafficking proteins can provide insights into the intracellular chemistry of reactive cofactors such as copper and zinc. Starting from the sequences of the metallochaperone Atx1 and from the first soluble domain of the copper-transporting ATPase Ccc2, both from yeast, a search on the available genomes was performed using a homology criterion and a metal-binding motif x`-x"-C-x'''-x⁗-C. By limiting ourselves to 20% identity with any of the proteins found, several soluble copper-transport proteins were identified, as well as soluble domains of membrane-bound ATPases. Structural models were calculated using high-resolution solution structures as templates, and the models were validated using statistical and energy criteria. Residue conservation and substitution have been interpreted and discussed in terms of structure-function relationship. The potential energy surfaces have been analyzed in terms of protein-protein interactions. We find that metallochaperones and their physiological partner ATPases from several phylogenetic kingdoms recognize one another, via an interplay of electrostatics, hydrogen bonding, and hydrophobic interactions, in a manner that precisely orients the metal-binding side chains for rapid metal transfer between otherwise tight binding sites. Finally, other putative metal-transport proteins are mentioned that have low homology and/or a different metal-binding consensus motif and that appear to use similar structures for recognition and transfer. This analysis highlights the wealth and the complexity of the field.

3 Present address: CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, Sesto Fiorentino, Florence, Italy 50019.

12:255-271 ©2002 by Cold Spring Harbor Laboratory Press  ISSN 1088-9051/02 $5.00
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
M. Gonzalez-Guerrero and J. M. Arguello
Mechanism of Cu+-transporting ATPases: Soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites
PNAS, April 22, 2008; 105(16): 5992 - 5997.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Banci, I. Bertini, S. Ciofi-Baffoni, A. Janicka, M. Martinelli, H. Kozlowski, and P. Palumaa
A Structural-Dynamical Characterization of Human Cox17
J. Biol. Chem., March 21, 2008; 283(12): 7912 - 7920.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
D. Magnani, O. Barre, S. D. Gerber, and M. Solioz
Characterization of the CopR Regulon of Lactococcus lactis IL1403
J. Bacteriol., January 15, 2008; 190(2): 536 - 545.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
J. C. Ebert and R. B. Altman
Robust recognition of zinc binding sites in proteins
Protein Sci., January 1, 2008; 17(1): 54 - 65.
[Abstract] [Full Text] [PDF]

Home page
 J. Med. Genet.Home page
P de Bie, P Muller, C Wijmenga, and L W J Klomp
Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes
J. Med. Genet., November 1, 2007; 44(11): 673 - 688.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
S. Lutsenko, N. L. Barnes, M. Y. Bartee, and O. Y. Dmitriev
Function and Regulation of Human Copper-Transporting ATPases
Physiol Rev, July 1, 2007; 87(3): 1011 - 1046.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. A. Yatsunyk and A. C. Rosenzweig
Cu(I) Binding and Transfer by the N Terminus of the Wilson Disease Protein
J. Biol. Chem., March 23, 2007; 282(12): 8622 - 8631.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Eren, D. C. Kennedy, M. J. Maroney, and J. M. Arguello
A Novel Regulatory Metal Binding Domain Is Present in the C Terminus of Arabidopsis Zn2+-ATPase HMA2
J. Biol. Chem., November 10, 2006; 281(45): 33881 - 33891.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Banci, I. Bertini, F. Cantini, N. DellaMalva, T. Herrmann, A. Rosato, and K. Wuthrich
Solution Structure and Intermolecular Interactions of the Third Metal-binding Domain of ATP7A, the Menkes Disease Protein
J. Biol. Chem., September 29, 2006; 281(39): 29141 - 29147.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Banci, I. Bertini, S. Ciofi-Baffoni, N. G. Kandias, N. J. Robinson, G. A. Spyroulias, X.-C. Su, S. Tottey, and M. Vanarotti
The delivery of copper for thylakoid import observed by NMR
PNAS, May 30, 2006; 103(22): 8320 - 8325.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. Achila, L. Banci, I. Bertini, J. Bunce, S. Ciofi-Baffoni, and D. L. Huffman
Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake
PNAS, April 11, 2006; 103(15): 5729 - 5734.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. K. Mandal, Y. Yang, T. M. Kertesz, and J. M. Arguello
Identification of the Transmembrane Metal Binding Site in Cu+-transporting PIB-type ATPases
J. Biol. Chem., December 24, 2004; 279(52): 54802 - 54807.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Banci, I. Bertini, S. Ciofi-Baffoni, X.-C. Su, G. P. M. Borrelly, and N. J. Robinson
Solution Structures of a Cyanobacterial Metallochaperone: INSIGHT INTO AN ATYPICAL COPPER-BINDING MOTIF
J. Biol. Chem., June 25, 2004; 279(26): 27502 - 27510.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
J. R. Prohaska and A. A. Gybina
Intracellular Copper Transport in Mammals
J. Nutr., May 1, 2004; 134(5): 1003 - 1006.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. M. Walker, D. Huster, M. Ralle, C. T. Morgan, N. J. Blackburn, and S. Lutsenko
The N-terminal Metal-binding Site 2 of the Wilson's Disease Protein Plays a Key Role in the Transfer of Copper from Atox1
J. Biol. Chem., April 9, 2004; 279(15): 15376 - 15384.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Banci, I. Bertini, S. Ciofi-Baffoni, L. Gonnelli, and X.-C. Su
Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis
J. Biol. Chem., December 12, 2003; 278(50): 50506 - 50513.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
J. L. Hall and L. E. Williams
Transition metal transporters in plants
J. Exp. Bot., December 1, 2003; 54(393): 2601 - 2613.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Arnesano, L. Banci, M. Benvenuti, I. Bertini, V. Calderone, S. Mangani, and M. S. Viezzoli
The Evolutionarily Conserved Trimeric Structure of CutA1 Proteins Suggests a Role in Signal Transduction
J. Biol. Chem., November 14, 2003; 278(46): 45999 - 46006.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Mana-Capelli, A. K. Mandal, and J. M. Arguello
Archaeoglobus fulgidus CopB Is a Thermophilic Cu2+-ATPase: FUNCTIONAL ROLE OF ITS HISTIDINE-RICH N-TERMINAL METAL BINDING DOMAIN
J. Biol. Chem., October 17, 2003; 278(42): 40534 - 40541.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. A. Roberts, G. F. Wildner, G. Grass, A. Weichsel, A. Ambrus, C. Rensing, and W. R. Montfort
A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase CueO
J. Biol. Chem., August 22, 2003; 278(34): 31958 - 31963.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Ralle, S. Lutsenko, and N. J. Blackburn
X-ray Absorption Spectroscopy of the Copper Chaperone HAH1 Reveals a Linear Two-coordinate Cu(I) Center Capable of Adduct Formation with Exogenous Thiols and Phosphines
J. Biol. Chem., June 13, 2003; 278(25): 23163 - 23170.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
L. A. Finney and T. V. O'Halloran
Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors
Science, May 9, 2003; 300(5621): 931 - 936.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
I. Bertini and A. Rosato
Bioinorganic Chemistry Special Feature: Bioinorganic chemistry in the postgenomic era
PNAS, April 1, 2003; 100(7): 3601 - 3604.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Li, B. P. Rosen, M. I. Borges-Walmsley, and A. R. Walmsley
Evidence for Cooperativity between the Four Binding Sites of Dimeric ArsD, an As(III)-responsive Transcriptional Regulator
J. Biol. Chem., July 12, 2002; 277(29): 25992 - 26002.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Genes Dev. Learn. Mem.
Protein Science RNA Genome Res.