1dmd: Difference between revisions

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[[Image:1dmd.gif|left|200px]]
{{Seed}}
[[Image:1dmd.png|left|200px]]


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{{STRUCTURE_1dmd|  PDB=1dmd  |  SCENE=  }}  
{{STRUCTURE_1dmd|  PDB=1dmd  |  SCENE=  }}  


'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF CALLINECTES SAPIDUS METALLOTHIONEIN-I DETERMINED BY HOMONUCLEAR AND HETERONUCLEAR MAGNETIC RESONANCE SPECTOSCOPY'''
===THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF CALLINECTES SAPIDUS METALLOTHIONEIN-I DETERMINED BY HOMONUCLEAR AND HETERONUCLEAR MAGNETIC RESONANCE SPECTOSCOPY===




==Overview==
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Metallothionein is a cysteine-rich metal-binding protein whose biosynthesis is closely regulated by the level of exposure of an organism to zinc, copper, cadmium, and other metal salts. The metallothionein from Callinectes sapidus is known to bind six divalent metal ions in two separate metal-binding clusters. Heteronuclear 1H-113Cd and homonuclear 1H-1H NMR correlation experiments have been used to establish that the two clusters reside in two distinct protein domains. The three-dimensional solution structure of the metallothionein has been determined using the distance and angle constraints derived from these two-dimensional NMR data sets and a distance geometry/simulated annealing protocol. There are no interdomain short distance (&lt; or = 4.5 A) constraints observed in this protein, enabling the calculation of structures for the N-terminal, beta domain and the C-terminal, alpha domain separately. A total of 18 structures were obtained for each domain. The structures are based on a total of 364 experimental NMR restraints consisting of 277 approximate interproton distance restraints, 12 chi 1 and 51 phi angular restraints, and 24 metal-to-cysteine connectivities obtained from 1H-113Cd correlation experiments. The only element of regular secondary structure in either of the two domains is a short segment of helix in the C-terminal alpha domain between Lys42 and Thr48. The folding of the polypeptide backbone chain in each domain, however, gives rise to several type I beta turns. There are no type II beta turns.
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{{ABSTRACT_PUBMED_7819257}}


==About this Structure==
==About this Structure==
1DMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Callinectes_sapidus Callinectes sapidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMD OCA].  
1DMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Callinectes_sapidus Callinectes sapidus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMD OCA].  


==Reference==
==Reference==
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[[Category: Narula, S S.]]
[[Category: Narula, S S.]]
[[Category: Metallothionein]]
[[Category: Metallothionein]]
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Revision as of 20:17, 30 June 2008

File:1dmd.png

Template:STRUCTURE 1dmd

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF CALLINECTES SAPIDUS METALLOTHIONEIN-I DETERMINED BY HOMONUCLEAR AND HETERONUCLEAR MAGNETIC RESONANCE SPECTOSCOPY

Template:ABSTRACT PUBMED 7819257

About this Structure

1DMD is a Single protein structure of sequence from Callinectes sapidus. Full experimental information is available from OCA.

Reference

Three-dimensional solution structure of Callinectes sapidus metallothionein-1 determined by homonuclear and heteronuclear magnetic resonance spectroscopy., Narula SS, Brouwer M, Hua Y, Armitage IM, Biochemistry. 1995 Jan 17;34(2):620-31. PMID:7819257

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