1sb6: Difference between revisions
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'''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1''' | {{Structure | ||
|PDB= 1sb6 |SIZE=350|CAPTION= <scene name='initialview01'>1sb6</scene> | |||
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'''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SB6 is a [ | 1SB6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SB6 OCA]. | ||
==Reference== | ==Reference== | ||
Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif., Banci L, Bertini I, Ciofi-Baffoni S, Su XC, Borrelly GP, Robinson NJ, J Biol Chem. 2004 Jun 25;279(26):27502-10. Epub 2004 Apr 8. PMID:[http:// | Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif., Banci L, Bertini I, Ciofi-Baffoni S, Su XC, Borrelly GP, Robinson NJ, J Biol Chem. 2004 Jun 25;279(26):27502-10. Epub 2004 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15075318 15075318] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
[[Category: spine]] | [[Category: spine]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
[[Category: structure]] | [[Category: structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:02:39 2008'' | ||
Revision as of 15:02, 20 March 2008
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Solution structure of a cyanobacterial copper metallochaperone, ScAtx1
OverviewOverview
The Atx1 copper metallochaperone from Synechocystis PCC 6803, ScAtx1, interacts with two P(1)-type copper ATPases to supply copper proteins within intracellular compartments, avoiding ATPases for other metals en route. Here we report NMR-derived solution structures for ScAtx1. The monomeric apo form has a betaalphabetabetaalpha fold with backbone motions largely restricted to loop 1 containing Cys-12 and Cys-15. The tumbling rate of Cu(I)ScAtx1 (0.1-0.8 mm) implies dimers. Experimental restraints are satisfied by symmetrical dimers with Cys-12 or His-61, but not Cys-15, invading the copper site of the opposing subunit. A full sequence of copper ligands from the cell surface to thylakoid compartments is proposed, considering in vitro homodimer liganding to mimic in vivo liganding in ScAtx1-ATPase heterodimers. A monomeric high resolution structure for Cu(I)ScAtx1, with Cys-12, Cys-15, and His-61 as ligands, is calculated without violations despite the rotational correlation time. (2)J(NH) couplings in the imidazole ring of His-61 establish coordination of N(epsilon2) to copper. His-61 is analogous to Lys-65 in eukaryotic metallochaperones, stabilizing Cu(I)S(2) complexes but by binding Cu(I) rather than compensating charge. Cys-Cys-His ligand sets are an emergent theme in some copper metallochaperones, although not in related Atx1, CopZ, or Hah1. Surface charge (Glu-13) close to the metal-binding site of ScAtx1 is likely to support interaction with complementary surfaces of copper-transporting ATPases (PacS-Arg-11 and CtaA-Lys-14) but to discourage interaction with zinc ATPase ZiaA and so inhibit aberrant formation of copper-ZiaA complexes.
About this StructureAbout this Structure
1SB6 is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
ReferenceReference
Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif., Banci L, Bertini I, Ciofi-Baffoni S, Su XC, Borrelly GP, Robinson NJ, J Biol Chem. 2004 Jun 25;279(26):27502-10. Epub 2004 Apr 8. PMID:15075318
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