1aqq
From Proteopedia
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[[Image:1aqq.jpg|left|200px]] | [[Image:1aqq.jpg|left|200px]] | ||
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'''AG-SUBSTITUTED METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, 10 STRUCTURES''' | '''AG-SUBSTITUTED METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, 10 STRUCTURES''' | ||
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[[Category: Narula, S S.]] | [[Category: Narula, S S.]] | ||
[[Category: Peterson, C W.]] | [[Category: Peterson, C W.]] | ||
- | [[Category: | + | [[Category: Copper detoxification]] |
- | [[Category: | + | [[Category: Metal-thiolate cluster]] |
- | [[Category: | + | [[Category: Metallothionein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:35:47 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:35, 2 May 2008
AG-SUBSTITUTED METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, 10 STRUCTURES
Overview
3D solution structural calculations for yeast silver(I)-substituted metallothionein (MT) and native copper(I) MT were completed using experimentally determined NOE and dihedral angle constraints, in conjunction with experimentally derived metal-to-Cys connectivities for AgMT which were assumed identical for CuMT. For the first 40 residues in both structures, the polypeptide backbone wraps around the metal cluster in two large parallel loops separated by a deep cleft containing the metal cluster. Minor differences between the two structures include differences in hydrogen bonds and the orientation of the N-terminus with the overall protein volume conserved to within 6.5%.
About this Structure
1AQQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
3D solution structure of copper and silver-substituted yeast metallothioneins., Peterson CW, Narula SS, Armitage IM, FEBS Lett. 1996 Jan 22;379(1):85-93. PMID:8566237 Page seeded by OCA on Fri May 2 10:35:47 2008