1m42: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m42 ConSurf].
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Revision as of 03:33, 8 February 2016

Solution structure of apoCopC from Pseudomonas syringaeSolution structure of apoCopC from Pseudomonas syringae

Structural highlights

1m42 is a 1 chain structure with sequence from Atcc 19310. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:COPC (ATCC 19310)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[COPC_PSEUB] Mediates copper resistance by sequestration of copper in the periplasm along with the copper-binding protein CopA.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the metal-free form of CopC, a protein involved in copper homeostasis, has been obtained. The fold is a Greek key beta barrel similar to that of functionally unrelated blue copper proteins but with important structural variations. The protein binds one equivalent of copper (II) with relatively high affinity and contains a cluster of conserved residues (His1, Glu27, Asp89, and His91) which could form a water-accessible metal binding site. The structure also reveals a loop containing the M(X)(n)M motif which is present in a number of proteins also involved in copper homeostasis. The present structure represents a link between copper-trafficking proteins and cupredoxins. Within a structural and genomic analysis, the role of CopC in copper trafficking is discussed.

Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis.,Arnesano F, Banci L, Bertini I, Thompsett AR Structure. 2002 Oct;10(10):1337-47. PMID:12377120[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Arnesano F, Banci L, Bertini I, Thompsett AR. Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis. Structure. 2002 Oct;10(10):1337-47. PMID:12377120
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