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2bb2

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X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS

Structural highlights

2bb2 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CRBB2_BOVIN Crystallins are the dominant structural components of the vertebrate eye lens.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, Blundell TL, Slingsby C. X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins. Nature. 1990 Oct 25;347(6295):776-80. PMID:2234050 doi:http://dx.doi.org/10.1038/347776a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bb2"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bb2' size='340' side='right'caption='[[2bb2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bb2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BB2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bb2]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BB2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb2 OCA], [https://pdbe.org/2bb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2bb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bb2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CRBB2_BOVIN CRBB2_BOVIN]] Crystallins are the dominant structural components of the vertebrate eye lens.
+[https://www.uniprot.org/uniprot/CRBB2_BOVIN CRBB2_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Bax, B]]
+[[Category: Bax B]]
-[[Category: Blundell, T L]]
+[[Category: Blundell TL]]
-[[Category: Driessen, H]]
+[[Category: Driessen H]]
-[[Category: Lapatto, R]]
+[[Category: Lapatto R]]
-[[Category: Lindley, P F]]
+[[Category: Lindley PF]]
-[[Category: Mahadevan, D]]
+[[Category: Mahadevan D]]
-[[Category: Nalini, V]]
+[[Category: Nalini V]]
-[[Category: Slingsby, C]]
+[[Category: Slingsby C]]
-[[Category: Eye lens protein]]

2bb2

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Current revision

X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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