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2bb2
From Proteopedia
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| - | [[Image:2bb2.jpg|left|200px]] | + | [[Image:2bb2.jpg|left|200px]] |
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| - | '''X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS''' | + | {{Structure |
| + | |PDB= 2bb2 |SIZE=350|CAPTION= <scene name='initialview01'>2bb2</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BB2 is a [ | + | 2BB2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB2 OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins., Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C, Nature. 1990 Oct 25;347(6295):776-80. PMID:[http:// | + | X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins., Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C, Nature. 1990 Oct 25;347(6295):776-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2234050 2234050] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: eye lens protein]] | [[Category: eye lens protein]] | ||
| - | ''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 15:59:36 2008'' |
Revision as of 13:59, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS
Overview
The beta, gamma-crystallins form a class of homologous proteins in the eye lens. Each gamma-crystallin comprises four topologically equivalent, Greek key motifs; pairs of motifs are organized around a local dyad to give domains and two similar domains are in turn related by a further local dyad. Sequence comparisons and model building predicted that hetero-oligomeric beta-crystallins also had internally quadruplicated subunits, but with extensions at the N and C termini, indicating that beta, gamma-crystallins evolved in two duplication steps from an ancestral protein folded as a Greek key. We report here the X-ray analysis at 2.1 A resolution of beta B2-crystallin homodimer which shows that the connecting peptide is extended and the two domains separated in a way quite unlike gamma-crystallin. Domain interactions analogous to those within monomeric gamma-crystallin are intermolecular and related by a crystallographic dyad in the beta B2-crystallin dimer. This shows how oligomers can evolve by conserving an interface rather than connectivity. A further interaction between dimers suggests a model for more complex aggregates of beta-crystallin in the lens.
About this Structure
2BB2 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins., Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C, Nature. 1990 Oct 25;347(6295):776-80. PMID:2234050
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