2bb2: Difference between revisions

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-[[Image:2bb2.jpg|left|200px]]
- {{Structure
+==X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS==
-|PDB= 2bb2 |SIZE=350|CAPTION= <scene name='initialview01'>2bb2</scene>, resolution 2.1&Aring;
+<StructureSection load='2bb2' size='340' side='right'caption='[[2bb2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb2 OCA], [http://www.ebi.ac.uk/pdbsum/2bb2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bb2 RCSB]</span>
+== Function ==
-}}
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/2bb2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bb2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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'''
+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<ref>PMID:2234050</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bb2" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Crystallin 3D structures|Crystallin 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-BB2 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].
+__TOC__
+</StructureSection>
-==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://www.ncbi.nlm.nih.gov/pubmed/2234050 2234050]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:03:45 2008''