2a5m

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[[Image:2a5m.gif|left|200px]]
 
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{{Structure
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==NMR structure of murine gamma-S crystallin from joint refinement with SAXS data==
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|PDB= 2a5m |SIZE=350|CAPTION= <scene name='initialview01'>2a5m</scene>
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<StructureSection load='2a5m' size='340' side='right'caption='[[2a5m]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= Crygs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1zwm|1ZWM]], [[1zwo|1ZWO]], [[1amm|1AMM]], [[1hk0|1HK0]], [[1a7h|1A7H]], [[1a45|1A45]], [[1ag4|1AG4]], [[1a5d|1A5D]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a5m OCA], [http://www.ebi.ac.uk/pdbsum/2a5m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a5m RCSB]</span>
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[https://www.uniprot.org/uniprot/CRYGS_MOUSE CRYGS_MOUSE] Crystallins are the dominant structural components of the vertebrate eye lens.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/2a5m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''NMR structure of murine gamma-S crystallin from joint refinement with SAXS data'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2a5m" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bax A]]
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[[Category: Bax, A.]]
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[[Category: Grishaev A]]
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[[Category: Grishaev, A.]]
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[[Category: Trewhella J]]
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[[Category: Trewhella, J.]]
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[[Category: Wu J]]
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[[Category: Wu, J.]]
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[[Category: alignment]]
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[[Category: deuteration]]
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[[Category: liquid crystal]]
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[[Category: mfr]]
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[[Category: molecular fragment replacement]]
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[[Category: pf1]]
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[[Category: rdc]]
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[[Category: residual dipolar coupling]]
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[[Category: sax]]
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[[Category: small-angle x-ray scattering]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:48:11 2008''
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Current revision

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

PDB ID 2a5m

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