1sb6: Difference between revisions

New page: left|200px<br /><applet load="1sb6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sb6" /> '''Solution structure of a cyanobacterial coppe...
 
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'''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1'''<br />
'''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1SB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SB6 OCA].  
1SB6 is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Banci, L.]]
[[Category: Banci, L.]]
[[Category: Bertini, I.]]
[[Category: Bertini, I.]]
[[Category: Borrelly, G.P.]]
[[Category: Borrelly, G P.]]
[[Category: Ciofi-Baffoni, S.]]
[[Category: Ciofi-Baffoni, S.]]
[[Category: Robinson, N.J.]]
[[Category: Robinson, N J.]]
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Su, X.C.]]
[[Category: Su, X C.]]
[[Category: copper chaperone]]
[[Category: copper chaperone]]
[[Category: new metal binding motif]]
[[Category: new metal binding motif]]
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[[Category: structure]]
[[Category: structure]]


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