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An atomic-level investigation of the disease-causing A629P mutant of the Menkes protein, ATP7A.

Banci L, Bertini I, Cantini F, Migliardi M, Rosato A, Wang S
J Mol Biol 352 409-17 (2005)
Related entries: 1yjr, 1yju, 1yjv

Cited: 25 times
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Abstract

Menkes disease is a fatal disease that can be induced by various mutations in the ATP7A gene, leading to unpaired uptake of dietary copper. The ATP7A gene encodes a copper(I)-translocating ATPase. Here the disease-causing A629P mutation, which occurs in the last of the six copper(I)-binding soluble domains of the ATPase (hereafter MNK6), was investigated. To understand why this apparently minor amino acid replacement is pathogenic, the solution structures and dynamics on various time-scales of wild-type and A629P-MNK6 were determined both in the apo- and copper(I)-loaded forms. The interaction in vitro with the physiological ATP7A copper(I)-donor (HAH1) was additionally studied. The A629P mutation makes the protein beta-sheet more solvent accessible, possibly resulting in an enhanced susceptibility of ATP7A to proteolytic cleavage and/or in reduced capability of copper(I)-translocation. A small reduction of the affinity for copper(I) is also observed. Both effects could concur to pathogenicity.

Reviews - 1yjt mentioned but not cited (1)

  1. Structural biology of copper trafficking. Boal AK, Rosenzweig AC. Chem Rev 109 4760-4779 (2009)

Articles - 1yjt mentioned but not cited (2)

  1. Modeling Structural Flexibility of Proteins with Go-Models. Jiang P, Hansmann UH. J Chem Theory Comput 8 2127-2133 (2012)
  2. Sampling of Protein Folding Transitions: Multicanonical Versus Replica Exchange Molecular Dynamics. Jiang P, Yaşar F, Hansmann UH. J Chem Theory Comput 9 (2013)


Reviews citing this publication (9)

  1. Function and regulation of human copper-transporting ATPases. Lutsenko S, Barnes NL, Bartee MY, Dmitriev OY. Physiol Rev 87 1011-1046 (2007)
  2. Cellular copper distribution: a mechanistic systems biology approach. Banci L, Bertini I, Cantini F, Ciofi-Baffoni S. Cell Mol Life Sci 67 2563-2589 (2010)
  3. An overview and update of ATP7A mutations leading to Menkes disease and occipital horn syndrome. Tümer Z. Hum Mutat 34 417-429 (2013)
  4. Biochemical basis of regulation of human copper-transporting ATPases. Lutsenko S, LeShane ES, Shinde U. Arch Biochem Biophys 463 134-148 (2007)
  5. Structural organization of human Cu-transporting ATPases: learning from building blocks. Barry AN, Shinde U, Lutsenko S. J Biol Inorg Chem 15 47-59 (2010)
  6. Molecular recognition in copper trafficking. Banci L, Bertini I, McGreevy KS, Rosato A. Nat Prod Rep 27 695-710 (2010)
  7. Mechanism of tumor resistance to cisplatin mediated by the copper transporter ATP7B. Dmitriev OY. Biochem Cell Biol 89 138-147 (2011)
  8. The MXCXXC class of metallochaperone proteins: model studies. Shoshan MS, Tshuva EY. Chem Soc Rev 40 5282-5292 (2011)
  9. Copper chaperone antioxidant 1: multiple roles and a potential therapeutic target. Yang D, Xiao P, Qiu B, Yu HF, Teng CB. J Mol Med (Berl) 101 527-542 (2023)

Articles citing this publication (13)

  1. The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Banci L, Bertini I, Cantini F, Felli IC, Gonnelli L, Hadjiliadis N, Pierattelli R, Rosato A, Voulgaris P. Nat Chem Biol 2 367-368 (2006)
  2. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Korotkov KV, Pardon E, Steyaert J, Hol WG. Structure 17 255-265 (2009)
  3. Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake. Achila D, Banci L, Bertini I, Bunce J, Ciofi-Baffoni S, Huffman DL. Proc Natl Acad Sci U S A 103 5729-5734 (2006)
  4. Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Banci L, Bertini I, Cantini F, Rosenzweig AC, Yatsunyk LA. Biochemistry 47 7423-7429 (2008)
  5. An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1. Banci L, Bertini I, Cantini F, Massagni C, Migliardi M, Rosato A. J Biol Chem 284 9354-9360 (2009)
  6. Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces. Banci L, Bertini I, Calderone V, Della-Malva N, Felli IC, Neri S, Pavelkova A, Rosato A. Biochem J 422 37-42 (2009)
  7. Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. LeShane ES, Shinde U, Walker JM, Barry AN, Blackburn NJ, Ralle M, Lutsenko S. J Biol Chem 285 6327-6336 (2010)
  8. Relating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule level. Benítez JJ, Keller AM, Huffman DL, Yatsunyk LA, Rosenzweig AC, Chen P. Faraday Discuss 148 71-82; discussion 97-108 (2011)
  9. Twenty-five novel mutations including duplications in the ATP7A gene. Moizard MP, Ronce N, Blesson S, Bieth E, Burglen L, Mignot C, Mortemousque I, Marmin N, Dessay B, Danesino C, Feillet F, Castelnau P, Toutain A, Moraine C, Raynaud M. Clin Genet 79 243-253 (2011)
  10. Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1. Banci L, Bertini I, Chasapis CT, Rosato A, Tenori L. Biochem Biophys Res Commun 364 645-649 (2007)
  11. The war of tools: how can NMR spectroscopists detect errors in their structures? Saccenti E, Rosato A. J Biomol NMR 40 251-261 (2008)
  12. ATP7A Clinical Genetics Resource - A comprehensive clinically annotated database and resource for genetic variants in ATP7A gene. Mhaske A, Dileep KV, Kumar M, Poojary M, Pandhare K, Zhang KYJ, Scaria V, Binukumar BK. Comput Struct Biotechnol J 18 2347-2356 (2020)
  13. A numerical investigation into possible mechanisms by that the A629P mutant of ATP7A causes Menkes Disease. Kouza M, Gowtham S, Seel M, Hansmann UH. Phys Chem Chem Phys 12 11390-11397 (2010)


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