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1ot4

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{{STRUCTURE_1ot4| PDB=1ot4 | SCENE= }}
{{STRUCTURE_1ot4| PDB=1ot4 | SCENE= }}
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'''Solution structure of Cu(II)-CopC from Pseudomonas syringae'''
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===Solution structure of Cu(II)-CopC from Pseudomonas syringae===
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==Overview==
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CopC from Pseudomonas syringae was found to be a protein capable of binding both Cu(I) and Cu(II) at two different sites. The solution structure of the apo protein is available, and structural information has been obtained on the Cu(I) bound form. We attempt here to set the limits for the determination of the solution structure of a Cu(II) protein, such as the Cu(II) bound form of CopC, in which the Cu(II) ion takes a type II coordination. The electron relaxation time is estimated from NMRD measurements to be 3 ns which leads to a correlation time for the nuclear spin-electron spin dipolar interaction of 2 ns. This information allowed us to tailor the NMR experiments and to fully exploit purely heteronuclear spectroscopy to assign as many signals as possible. In this way, 37 (13)C and 11 (15)N signals that completely escape detection with conventional approaches were assigned. Paramagnetic based structural constraints were obtained by measuring paramagnetic longitudinal relaxation enhancements (rho(para)) which allowed us to precisely locate the copper ion within the protein frame. Pseudocontact shifts (pcs's) were also used as constraints for 83 (1)H and 18 (13)C nuclei. With them, together with other standard structural constraints, a structure is obtained (and submitted to PDB) where information is only missing in a sphere with a 6 A radius from the copper ion. If we borrow information from EXAFS data, which show evidence of two copper coordinated histidines, then His 1 and His 91 are unambiguously identified as copper ligands. EXAFS data indicate two more light donor atoms (O/N) which could be from Asp 27 and Glu 89, whereas the NMRD data indicate the presence of a semicoordinated water molecule at 2.8 A (Cu-O distance) roughly orthogonal to the plane identified by the other four ligands. This represents the most extensively characterized structure of a type II Cu(II) protein obtained employing the most advanced NMR methods and with the aid of EXAFS data. The knowledge of the location of the Cu(II) in the protein is important for the copper transfer mechanism.
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{{ABSTRACT_PUBMED_12797793}}
==About this Structure==
==About this Structure==
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1OT4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT4 OCA].
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1OT4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT4 OCA].
==Reference==
==Reference==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:09:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:36:12 2008''

Revision as of 16:36, 27 July 2008

Image:1ot4.png

Template:STRUCTURE 1ot4

Solution structure of Cu(II)-CopC from Pseudomonas syringae

Template:ABSTRACT PUBMED 12797793

About this Structure

1OT4 is a Single protein structure of sequence from Pseudomonas syringae. Full experimental information is available from OCA.

Reference

A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae., Arnesano F, Banci L, Bertini I, Felli IC, Luchinat C, Thompsett AR, J Am Chem Soc. 2003 Jun 18;125(24):7200-8. PMID:12797793

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