This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dsl
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==GAMMA B CRYSTALLIN C-TERMINAL DOMAIN== | ==GAMMA B CRYSTALLIN C-TERMINAL DOMAIN== | ||
| - | <StructureSection load='1dsl' size='340' side='right' caption='[[1dsl]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='1dsl' size='340' side='right'caption='[[1dsl]], [[Resolution|resolution]] 1.55Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dsl]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1dsl]] 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=1DSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DSL FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <table> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsl OCA], [https://pdbe.org/1dsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dsl RCSB], [https://www.ebi.ac.uk/pdbsum/1dsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsl ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsl_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/1dsl_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1dsl ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice. | ||
| - | |||
| - | The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins.,Norledge BV, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HP Nat Struct Biol. 1996 Mar;3(3):267-74. PMID:8605629<ref>PMID:8605629</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Crystallin 3D structures|Crystallin 3D structures]] | |
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Bateman | + | [[Category: Large Structures]] |
| - | [[Category: Driessen | + | [[Category: Bateman OA]] |
| - | [[Category: Glockshuber | + | [[Category: Driessen HPC]] |
| - | [[Category: Jaenicke | + | [[Category: Glockshuber R]] |
| - | [[Category: Mayr | + | [[Category: Jaenicke R]] |
| - | [[Category: Norledge | + | [[Category: Mayr E-M]] |
| - | [[Category: Slingsby | + | [[Category: Norledge BV]] |
| - | + | [[Category: Slingsby C]] | |
| - | + | ||
Current revision
GAMMA B CRYSTALLIN C-TERMINAL DOMAIN
| |||||||||||
