|
|
| Line 1: |
Line 1: |
| [[Image:1sb6.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1sb6.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1sb6| PDB=1sb6 | SCENE= }} | | {{STRUCTURE_1sb6| PDB=1sb6 | SCENE= }} |
|
| |
|
| '''Solution structure of a cyanobacterial copper metallochaperone, ScAtx1'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15075318}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15075318 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15075318}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 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]. | | 1SB6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SB6 OCA]. |
|
| |
|
| ==Reference== | | ==Reference== |
| Line 36: |
Line 40: |
| [[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 Sun Apr 13 08:10:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:09:37 2008'' |