View source for 2jyp


==Coordinates for lowest energy structure of Aragonite protein-7, C-terminal domain==
<StructureSection load='2jyp' size='340' side='right'caption='[[2jyp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jyp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JYP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=2jyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jyp OCA], [https://pdbe.org/2jyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jyp RCSB], [https://www.ebi.ac.uk/pdbsum/2jyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jyp ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The RING or Really Interesting New Gene represents a family of eukaryotic sequences that bind Zn (II) ions and participate in intracellular processes involving protein-protein interaction. Although found in over 400 different proteins, very little is known regarding the structure-function properties of these domains because of the aggregation problems associated with RING sequences. To augment this data set, we report an unusual 36 AA C-terminal sequence of an extracellular matrix mollusk shell protein, AP7, that exhibits partial homology to the RING family. This Cys, His-containing sequence, termed AP7C, binds Zn (II) and other multivalent ions, but does not utilize a tetracoordinate complexation scheme for binding such as that found in Zn (II) finger polypeptides. Moreover, unlike Zn (II) finger and RING domains, this 36 AA can fold into a relatively stable structure in the absence of Zn (II). This folded structure consists of three short helical segments (A, B, and C), with segments A and B separated by a 4 AA type I beta-turn region and segments B and C separated by a 7 AA loop-like region. Interestingly, the putative RING-like region, -RRPFHECALCYSI-, experiences slow conformational exchange between two structural states in solution, most likely in response to imido ring interconversion at P8 and P21. Poisson-Boltzmann solvation calculations reveal that the AP7C molecular surface possesses a cationic region near its N-terminus, which lies adjacent to the 30 AA mineral modification domain in the AP7 protein. Given that the AP7C sequence does not influence mineralization, it is probable that this cationic pseudo-RING region is utilized by the AP7 protein for other tasks such as protein-protein interaction within the mollusk shell matrix.

Identification and Structural Characterization of an Unusual RING-Like Sequence within an Extracellular Biomineralization Protein, AP7.,Collino S, Kim IW, Evans JS Biochemistry. 2008 Mar 25;47(12):3745-55. Epub 2008 Feb 26. PMID:18298090<ref>PMID:18298090</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jyp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Haliotis rufescens]]
[[Category: Large Structures]]
[[Category: Collino S]]
[[Category: Evans J]]
[[Category: Kim I]]