1prr

<StructureSection load='1prr' size='340' side='right'caption='[[1prr]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRR FirstGlance]. <br>

</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1prs|1prs]]</div></td></tr>

[[https://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA]] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.

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== Publication Abstract from PubMed ==

BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.

NMR-derived three-dimensional solution structure of protein S complexed with calcium.,Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M Structure. 1994 Feb 15;2(2):107-22. PMID:8081742<ref>PMID:8081742</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1prr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 25232]]

[[Category: Bagby, S]]

[[Category: Eagle, S G]]

[[Category: Harvey, T S]]

[[Category: Ikura, M]]

[[Category: Inouye, S]]

[[Category: Binding protein]]