1nps: Difference between revisions
New page: left|200px<br /><applet load="1nps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nps, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ... |
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== | ==CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF PROTEIN S== | ||
Protein S from Myxococcus xanthus is a member of the beta gamma-crystallin | <StructureSection load='1nps' size='340' side='right'caption='[[1nps]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NPS 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]] 1.8Å</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=1nps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nps OCA], [https://pdbe.org/1nps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nps RCSB], [https://www.ebi.ac.uk/pdbsum/1nps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nps 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/np/1nps_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=1nps ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein S from Myxococcus xanthus is a member of the beta gamma-crystallin superfamily. Its N and C-terminal domains (NPS and CPS, respectively) show a high degree of structural similarity and possess the capacity to bind two calcium ions per domain. For NPS, their positions were determined by X-ray diffraction at 1.8 A resolution, making use of molecular replacement with the NMR structure as search model. The overall topology of NPS is found to be practically the same as in complete protein S. In natural protein S, the domains fold independently, with a significant increase in stability and cooperativity of folding in the presence of Ca2+. The recombinant isolated domains are stable monomers which do not show any tendency to combine to "nicked" full-length protein S. In order to investigate the stability and folding of natural protein S and its isolated domains, spectroscopic techniques were applied, measuring the reversible urea and temperature-induced unfolding transitions at varying pH. The increment of Ca2+ to the free energy of stabilization amounts to -10 and -5 kJ/mol for NPS and CPS, respectively. For both NPS and CPS, in the absence and in the presence of 3 mM CaCl2, the two-state model is valid. Comparing DeltaGU-->N for CPS (-21 kJ/mol at pH 7, liganded with Ca2+) with its increment in the intact two-domain protein, the stability of the isolated domain turns out to be decreased in a pH-dependent manner. In contrast, the stability of Ca2+-loaded NPS (DeltaGU-->N=-31 kJ/mol, pH 7) is nearly unchanged down to pH 2 where Ca2+ is released (DeltaGU-->N=-26 kJ/mol, pH 2). In intact protein S, the N-terminal domain is destabilized relative to NPS. Evidently, apart from Ca2+ binding, well-defined domain interactions contribute significantly to the overall stability of intact protein S. | |||
The domains of protein S from Myxococcus xanthus: structure, stability and interactions.,Wenk M, Baumgartner R, Holak TA, Huber R, Jaenicke R, Mayr EM J Mol Biol. 1999 Mar 12;286(5):1533-45. PMID:10064714<ref>PMID:10064714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nps" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Laccase 3D structures|Laccase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Myxococcus xanthus]] | [[Category: Myxococcus xanthus]] | ||
[[Category: Baumgartner R]] | |||
[[Category: Baumgartner | [[Category: Holak TA]] | ||
[[Category: Holak | [[Category: Huber R]] | ||
[[Category: Huber | [[Category: Jaenicke R]] | ||
[[Category: Jaenicke | [[Category: Mayer EM]] | ||
[[Category: Mayer | [[Category: Wenk M]] | ||
[[Category: Wenk | |||
