1prr: Difference between revisions
New page: left|200px<br /><applet load="1prr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prr" /> '''NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUC... |
No edit summary |
||
| (15 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM== | ||
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding | <StructureSection load='1prr' size='340' side='right'caption='[[1prr]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [https://pdbe.org/1prr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [https://www.ebi.ac.uk/pdbsum/1prr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1prr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1prr ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1prr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Myxococcus xanthus]] | [[Category: Myxococcus xanthus]] | ||
[[Category: Bagby S]] | |||
[[Category: Bagby | [[Category: Eagle SG]] | ||
[[Category: Eagle | [[Category: Harvey TS]] | ||
[[Category: Harvey | [[Category: Ikura M]] | ||
[[Category: Ikura | [[Category: Inouye S]] | ||
[[Category: Inouye | |||
Latest revision as of 12:00, 22 May 2024
NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUMNMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM
Structural highlights
FunctionDESS_MYXXA Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||||