1sb6
From Proteopedia
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'''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1''' | '''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1''' | ||
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[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Su, X C.]] | [[Category: Su, X C.]] | ||
- | [[Category: | + | [[Category: Copper chaperone]] |
- | [[Category: | + | [[Category: New metal binding motif]] |
- | [[Category: | + | [[Category: Nmr]] |
- | [[Category: | + | [[Category: Spine]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Structural proteomics in europe]] |
- | [[Category: | + | [[Category: Structure]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:10:51 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun | + |
Revision as of 05:10, 13 April 2008
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 Page seeded by OCA on Sun Apr 13 08:10:51 2008
Categories: Single protein | Synechocystis sp. | Banci, L. | Bertini, I. | Borrelly, G P. | Ciofi-Baffoni, S. | Robinson, N J. | SPINE, Structural Proteomics in Europe. | Su, X C. | Copper chaperone | New metal binding motif | Nmr | Spine | Structural genomic | Structural proteomics in europe | Structure