3hz2: Difference between revisions
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==Crystal structure of a betagamma-crystallin from an Archaea== | ==Crystal structure of a betagamma-crystallin from an Archaea== | ||
<StructureSection load='3hz2' size='340' side='right' caption='[[3hz2]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='3hz2' size='340' side='right'caption='[[3hz2]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hz2]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3hz2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZ2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hz2 OCA], [https://pdbe.org/3hz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hz2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hz2 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8TMX3_METAC Q8TMX3_METAC] | |||
== 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/hz/3hz2_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/3hz2_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=3hz2 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3hz2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Crystallin 3D structures|Crystallin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Methanosarcina acetivorans]] | [[Category: Methanosarcina acetivorans]] | ||
[[Category: Aravind | [[Category: Aravind P]] | ||
[[Category: Sankaranarayanan | [[Category: Sankaranarayanan R]] | ||
Latest revision as of 18:54, 1 November 2023
Crystal structure of a betagamma-crystallin from an ArchaeaCrystal structure of a betagamma-crystallin from an Archaea
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe betagamma-crystallin superfamily consists of evolutionarily related proteins with domain topology similar to lens beta- and gamma-crystallins, formed from duplicated Greek key motifs. Ca2+-binding was found in a few betagamma-crystallin members earlier, although its prevalence and diversity as an inherent molecular property among members of the superfamily is not well-studied. To increase our understanding of Ca2+-binding in various betagamma-crystallins, we undertook comprehensive structural and Ca2+-binding studies of seven members of the superfamily from bacteria, archaea and vertebrates, including determination of high resolution crystal structures of three proteins. Our structural observations show that the determinants of Ca2+ coordination remain conserved in the form of an N/D-N/D-#-I-S/T-S motif in all domains. However, binding of Ca2+ elicits varied physico-chemical responses, ranging from passive sequestration to active stabilization. The motif in this superfamily is modified in some members like lens crystallins where Ca2+-binding abilities are partly or completely compromised. We show that reduction or loss of Ca2+-binding in members of the superfamily, particularly in vertebrates, is due to the selective presence of unfavorable amino acids (largely Arg) at key Ca2+-ligation positions and that engineering of the canonical Ca2+-binding residues can confer binding activity on an otherwise inactive domain. Through this work, we demonstrate that betagamma-crystallins with the N/D-N/D-#-I-S/T-S motif form an extensive set of Ca2+-binding proteins prevalent in all the three kingdoms of life. betagamma-Crystallin superfamily contains a universal motif for binding calcium.,Aravind P, Mishra A, Suman SK, Jobby MK, Sankaranarayanan R, Sharma Y Biochemistry. 2009 Nov 18. PMID:19921810[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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