1sb6

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sb6 OCA], [http://www.ebi.ac.uk/pdbsum/1sb6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sb6 RCSB]</span>
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[[Category: structure]]
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Revision as of 20:39, 30 March 2008

Image:1sb6.jpg


PDB ID 1sb6

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution structure of a cyanobacterial copper metallochaperone, ScAtx1


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.

About this Structure

1SB6 is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

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:15075318

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