1e7n: Difference between revisions
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'''THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER''' | {{Structure | ||
|PDB= 1e7n |SIZE=350|CAPTION= <scene name='initialview01'>1e7n</scene>, resolution 2.35Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E7N is a [ | 1E7N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7N OCA]. | ||
==Reference== | ==Reference== | ||
The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer., Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C, J Mol Biol. 2000 Dec 1;304(3):253-7. PMID:[http:// | The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer., Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C, J Mol Biol. 2000 Dec 1;304(3):253-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11090271 11090271] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Wieligmann, K.]] | [[Category: Wieligmann, K.]] | ||
[[Category: 2-fold symmetry]] | [[Category: 2-fold symmetry]] | ||
[[Category: | [[Category: crystallin]] | ||
[[Category: domain | [[Category: domain interaction]] | ||
[[Category: eye lens]] | [[Category: eye lens]] | ||
[[Category: protein structure]] | [[Category: protein structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:11 2008'' | ||
Revision as of 08:51, 20 March 2008
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| 1e7n, resolution 2.35Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER
Overview
betagamma-crystallins from the eye lens are proteins consisting of two similar domains joined by a short linker. All three-dimensional structures of native proteins solved so far reveal similar pseudo-2-fold pairing of the domains reflecting their presumed ancient origin from a single-domain homodimer. However, studies of engineered single domains of members of the betagamma-crystallin superfamily have not revealed a prototype ancestral solution homodimer. Here we report the 2.35 A X-ray structure of the homodimer of the N-terminal domain of rat betaB2-crystallin (betaB2-N). The two identical domains pair in a symmetrical manner very similar to that observed in native betagamma-crystallins, where N and C-terminal domains (which share approximately 35% sequence identity) are related by a pseudo-2-fold axis. betaB2-N thus resembles the ancestral prototype of the betagamma-crystallin superfamily as it self-associates in solution to form a dimer with an essentially identical domain interface as that between the N and C domains in betagamma-crystallins, but without the benefit of a covalent linker. The structure provides further evidence for the role of two-domain pairing in stabilising the protomer fold. These results support the view that the betagamma-crystallin superfamily has evolved by a series of gene duplication and fusion events from a single-domain ancestor capable of forming homodimers.
About this Structure
1E7N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer., Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C, J Mol Biol. 2000 Dec 1;304(3):253-7. PMID:11090271
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