5z6d

<table><tr><td colspan='2'>[[5z6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neucr Neucr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z6D FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">app, NCU04533 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367110 NEUCR])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z6d OCA], [http://pdbe.org/5z6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z6d RCSB], [http://www.ebi.ac.uk/pdbsum/5z6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z6d ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

We describe a set of proteins in which a betagamma-crystallin domain pairs with an Ig-like domain, and which are confined to microbes, like bacteria, slime molds and fungi. DdCAD-1 (Ca(2+) -dependent cell adhesion molecule-1) and abundant perithecial protein (APP) represent this class of molecules. Using the crystal structure of APP-NTD (N-terminal domain of APP), we describe its mode of Ca(2+) binding and provide a generalized theme for correct identification of the Ca(2+) -binding site within this class of molecules. As a common feature, one of the two Ca(2+) -binding sites is non-functional in the betagamma-crystallin domains of these proteins. While APP-NTD binds Ca(2+) with a micromolar affinity which is comparable to DdCAD-1, APP surprisingly does not bind Ca(2+) . Crystal structures of APP and Ca(2+) -bound APP-NTD reveal that the interface interactions in APP render its Ca(2+) -binding site inoperative. Thus, heterodomain association provides a novel mode of Ca(2+) -binding regulation in APP. Breaking the interface interactions (mutating Asp30Ala, Leu132Ala and Ile135Ala) or separation from the Ig-like domain removes the constraints upon the required conformational transition and enables the betagamma-crystallin domain to bind Ca(2+) . In mechanistic detail, our work demonstrates an interdomain interface adapted to distinct functional niches in APP and its homolog DdCAD-1.

 

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== References ==

[[Category: Neucr]]

[[Category: Sankaranarayanan, R]]

[[Category: Srivastava, S S]]

[[Category: Metal binding protein]]