1ag4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /><applet load="1ag4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ag4" /> '''NMR STRUCTURE OF SPHERULIN 3A (S3A) FROM PHY...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ag4.gif|left|200px]]<br /><applet load="1ag4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ag4" />
'''NMR STRUCTURE OF SPHERULIN 3A (S3A) FROM PHYSARUM POLYCEPHALUM, MINIMIZED AVERAGE STRUCTURE'''<br />


==Overview==
==NMR STRUCTURE OF SPHERULIN 3A (S3A) FROM PHYSARUM POLYCEPHALUM, MINIMIZED AVERAGE STRUCTURE==
Spherulin 3a is the most abundantly expressed cytosolic protein in, spherulating plasmodia of the slime mold Physarum polycephalum. High, yields of unlabeled, uniformly 15N and uniformly 13C/15N-labeled, recombinant spherulin 3a from Escherichia coli could be produced by a, simple protocol described here. The three-dimensional solution structure, of Ca2+-loaded spherulin 3a was determined by homo- and heteronuclear NMR, spectroscopy. The structure of monomeric spherulin 3a consists of two, pleated beta-sheets plus a short alpha-helix arranged into the, gamma-crystallin fold. The beta-sheets comprise two intertwined Greek-key, motifs. An additional N-terminal beta-strand is unique to spherulin 3a., Complexation of calcium ions greatly enhances overall conformational, stability of the protein. The average atomic root-mean-square deviations, (r.m.s.d.) for heavy atoms in beta-strands were 0.34(+/-0.16) A for the, backbone atoms and 0.73(+/-0.40) A for all atoms. The corresponding, r.m.s.d. values for heavy atoms in the whole protein were 0.62(+/-0.42) A, for the backbone atoms and 0.99(+/-0.65) A for all atoms. We show the, structural relationship between spherulin 3a, a myxomycete dormancy, protein, and crystallins from the vertebrate eye lens. Since spherulin 3a, has a structure corresponding to one domain of bovine, gammaB(II)-crystallin, it represents a hypothetical ancestral, gamma-crystallin precursor structure.
<StructureSection load='1ag4' size='340' side='right'caption='[[1ag4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ag4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AG4 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ag4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ag4 OCA], [https://pdbe.org/1ag4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ag4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ag4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ag4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SR3A_PHYPO SR3A_PHYPO] Structural protein.
== 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/ag/1ag4_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=1ag4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spherulin 3a is the most abundantly expressed cytosolic protein in spherulating plasmodia of the slime mold Physarum polycephalum. High yields of unlabeled, uniformly 15N and uniformly 13C/15N-labeled recombinant spherulin 3a from Escherichia coli could be produced by a simple protocol described here. The three-dimensional solution structure of Ca2+-loaded spherulin 3a was determined by homo- and heteronuclear NMR spectroscopy. The structure of monomeric spherulin 3a consists of two pleated beta-sheets plus a short alpha-helix arranged into the gamma-crystallin fold. The beta-sheets comprise two intertwined Greek-key motifs. An additional N-terminal beta-strand is unique to spherulin 3a. Complexation of calcium ions greatly enhances overall conformational stability of the protein. The average atomic root-mean-square deviations (r.m.s.d.) for heavy atoms in beta-strands were 0.34(+/-0.16) A for the backbone atoms and 0.73(+/-0.40) A for all atoms. The corresponding r.m.s.d. values for heavy atoms in the whole protein were 0.62(+/-0.42) A for the backbone atoms and 0.99(+/-0.65) A for all atoms. We show the structural relationship between spherulin 3a, a myxomycete dormancy protein, and crystallins from the vertebrate eye lens. Since spherulin 3a has a structure corresponding to one domain of bovine gammaB(II)-crystallin, it represents a hypothetical ancestral gamma-crystallin precursor structure.


==About this Structure==
Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution.,Rosinke B, Renner C, Mayr EM, Jaenicke R, Holak TA J Mol Biol. 1997 Aug 29;271(4):645-55. PMID:9281431<ref>PMID:9281431</ref>
1AG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AG4 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution., Rosinke B, Renner C, Mayr EM, Jaenicke R, Holak TA, J Mol Biol. 1997 Aug 29;271(4):645-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9281431 9281431]
</div>
<div class="pdbe-citations 1ag4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
[[Category: Single protein]]
[[Category: Holak TA]]
[[Category: Holak, T.A.]]
[[Category: Jaenicke R]]
[[Category: Jaenicke, R.]]
[[Category: Mayr E-M]]
[[Category: Mayr, E.M.]]
[[Category: Renner C]]
[[Category: Renner, C.]]
[[Category: Rosinke B]]
[[Category: Rosinke, B.]]
[[Category: spherulation-specific protein]]
[[Category: structural protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:49:38 2007''
Retrieved from "https://proteopedia.org/1ag4"