View source for 3sny


==Crystal structure of a mutant T82R of a betagamma-crystallin domain from Clostridium beijerinckii==
<StructureSection load='3sny' size='340' side='right'caption='[[3sny]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sny]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii_NCIMB_8052 Clostridium beijerinckii NCIMB 8052]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SNY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3sny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sny OCA], [https://pdbe.org/3sny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sny RCSB], [https://www.ebi.ac.uk/pdbsum/3sny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sny ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A6LX94_CLOB8 A6LX94_CLOB8] 
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== Publication Abstract from PubMed ==
Numerous proteins belonging to the recently expanded betagamma-crystallin superfamily bind Ca(2+) at the double-clamp N/D-N/D-X(1)-X(2)-S/T-S motif. However, there have been no attempts to understand the intricacies involving Ca(2+) binding, such as the determinants of Ca(2+)-binding affinity and their contributions to gain in stability. This work is an in-depth analysis of understanding the modes and determinants of Ca(2+) binding to betagamma-crystallin motifs. We have performed extensive naturally occurring substitutions from related proteins on the betagamma-crystallin domains of flavollin, a low-affinity Ca(2+)-binding protein, and clostrillin, a moderate-affinity protein. We monitored the consequences of these modifications on Ca(2)(+) binding by isothermal titration calorimetry, thermal stability and conformational and crystal structure analyses. We demonstrate that Ca(2)(+) binding to the two sites of a betagamma-domain is interdependent and that the presence of Arg at the fifth position disables a site. A change from Thr to Ser, or vice versa, influences Ca(2+)-binding affinity, highlighting the basis of diversity found in these domains. A subtle change in the first site has a greater influence on Ca(2)(+) binding than a similar alteration in the second site. Thus, the second site is more variable in nature. Replacing an acidic or hydrophobic residue in a binding site alters the Ca(2+)-binding properties drastically. While it appears from their binding site sequence that these domains have evolved randomly, our examination illustrates the subtlety in the design of these modules. Decoding such design schemes would aid in our understanding of the functional themes underlying differential Ca(2)(+) binding and in predicting these in emerging sequence information.

Decoding the molecular design principles underlying Ca(2+) binding to betagamma-crystallin motifs.,Mishra A, Suman SK, Srivastava SS, Sankaranarayanan R, Sharma Y J Mol Biol. 2012 Jan 6;415(1):75-91. Epub 2011 Oct 31. PMID:22099475<ref>PMID:22099475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Clostridium beijerinckii NCIMB 8052]]
[[Category: Large Structures]]
[[Category: Sankaranarayanan R]]
[[Category: Srivastava SS]]