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[[Image:2a5m.gif|left|200px]]
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{{STRUCTURE_2a5m|  PDB=2a5m  |  SCENE=  }}
'''NMR structure of murine gamma-S crystallin from joint refinement with SAXS data'''


==NMR structure of murine gamma-S crystallin from joint refinement with SAXS data==
<StructureSection load='2a5m' size='340' side='right'caption='[[2a5m]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a5m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A5M 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=2a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a5m OCA], [https://pdbe.org/2a5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a5m RCSB], [https://www.ebi.ac.uk/pdbsum/2a5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a5m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRYGS_MOUSE CRYGS_MOUSE] Crystallins are the dominant structural components of the vertebrate eye lens.
== 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/a5/2a5m_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=2a5m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Determination of the 3D structures of multidomain proteins by solution NMR methods presents a number of unique challenges related to their larger molecular size and the usual scarcity of constraints at the interdomain interface, often resulting in a decrease in structural accuracy. In this respect, experimental information from small-angle scattering of X-ray radiation in solution (SAXS) presents a suitable complement to the NMR data, as it provides an independent constraint on the overall molecular shape. A computational procedure is described that allows incorporation of such SAXS data into the mainstream high-resolution macromolecular structure refinement. The method is illustrated for a two-domain 177-amino-acid protein, gammaS crystallin, using an experimental SAXS data set fitted at resolutions from approximately 200 A to approximately 30 A. Inclusion of these data during structure refinement decreases the backbone coordinate root-mean-square difference between the derived model and the high-resolution crystal structure of a 54% homologous gammaB crystallin from 1.96 +/- 0.07 A to 1.31 +/- 0.04 A. Combining SAXS data with NMR restraints can be accomplished at a moderate computational expense and is expected to become useful for multidomain proteins, multimeric assemblies, and tight macromolecular complexes.


==Overview==
Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data.,Grishaev A, Wu J, Trewhella J, Bax A J Am Chem Soc. 2005 Nov 30;127(47):16621-8. PMID:16305251<ref>PMID:16305251</ref>
Determination of the 3D structures of multidomain proteins by solution NMR methods presents a number of unique challenges related to their larger molecular size and the usual scarcity of constraints at the interdomain interface, often resulting in a decrease in structural accuracy. In this respect, experimental information from small-angle scattering of X-ray radiation in solution (SAXS) presents a suitable complement to the NMR data, as it provides an independent constraint on the overall molecular shape. A computational procedure is described that allows incorporation of such SAXS data into the mainstream high-resolution macromolecular structure refinement. The method is illustrated for a two-domain 177-amino-acid protein, gammaS crystallin, using an experimental SAXS data set fitted at resolutions from approximately 200 A to approximately 30 A. Inclusion of these data during structure refinement decreases the backbone coordinate root-mean-square difference between the derived model and the high-resolution crystal structure of a 54% homologous gammaB crystallin from 1.96 +/- 0.07 A to 1.31 +/- 0.04 A. Combining SAXS data with NMR restraints can be accomplished at a moderate computational expense and is expected to become useful for multidomain proteins, multimeric assemblies, and tight macromolecular complexes.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2A5M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5M OCA].
</div>
<div class="pdbe-citations 2a5m" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data., Grishaev A, Wu J, Trewhella J, Bax A, J Am Chem Soc. 2005 Nov 30;127(47):16621-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16305251 16305251]
*[[Crystallin 3D structures|Crystallin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Bax A]]
[[Category: Bax, A.]]
[[Category: Grishaev A]]
[[Category: Grishaev, A.]]
[[Category: Trewhella J]]
[[Category: Trewhella, J.]]
[[Category: Wu J]]
[[Category: Wu, J.]]
[[Category: Alignment]]
[[Category: Deuteration]]
[[Category: Liquid crystal]]
[[Category: Mfr]]
[[Category: Molecular fragment replacement]]
[[Category: Pf1]]
[[Category: Rdc]]
[[Category: Residual dipolar coupling]]
[[Category: Sax]]
[[Category: Small-angle x-ray scattering]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:38:22 2008''

Latest revision as of 08:15, 15 May 2024

NMR structure of murine gamma-S crystallin from joint refinement with SAXS data

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