1i5i

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[[Image:1i5i.gif|left|200px]]
 
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==THE C18S MUTANT OF BOVINE (GAMMA-B)-CRYSTALLIN==
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The line below this paragraph, containing "STRUCTURE_1i5i", creates the "Structure Box" on the page.
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<StructureSection load='1i5i' size='340' side='right'caption='[[1i5i]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1i5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I5I FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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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=1i5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i5i OCA], [https://pdbe.org/1i5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i5i RCSB], [https://www.ebi.ac.uk/pdbsum/1i5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i5i ProSAT]</span></td></tr>
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{{STRUCTURE_1i5i| PDB=1i5i | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
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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/i5/1i5i_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=1i5i 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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The cysteine residues of the gamma crystallins, a family of ocular lens proteins, are involved in the aggregation and phase separation of these proteins. Both these phenomena are implicated in cataract formation. We have used bovine gammaB crystallin as a model system to study the role of the individual cysteine residues in the aggregation and phase separation of the gamma crystallins. Here, we compare the thermodynamic and kinetic behavior of the recombinant wild-type protein (WT) and the Cys18 to Ser (C18S) mutant. We find that the solubilities of the two proteins are similar. The kinetics of crystallization, however, are different. The WT crystallizes slowly enough for the metastable liquid-liquid coexistence to be easily observed. C18S, on the other hand, crystallizes rapidly; the metastable coexisting liquid phases of the pure mutant do not form. Nevertheless, the coexistence curve of C18S can be determined provided that crystallization is kinetically suppressed. In this way we found that the coexistence curve coincides with that of the WT. Despite the difference in the kinetics of crystallization, the two proteins were found to have the same crystal forms and almost identical X-ray structures. Our results demonstrate that even conservative point mutations can bring about dramatic changes in the kinetics of crystallization. The implications of our findings for cataract formation and protein crystallization are discussed.
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'''THE C18S MUTANT OF BOVINE (GAMMA-B)-CRYSTALLIN'''
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Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin.,Asherie N, Pande J, Pande A, Zarutskie JA, Lomakin J, Lomakin A, Ogun O, Stern LJ, King J, Benedek GB J Mol Biol. 2001 Dec 7;314(4):663-9. PMID:11733987<ref>PMID:11733987</ref>
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==Overview==
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The cysteine residues of the gamma crystallins, a family of ocular lens proteins, are involved in the aggregation and phase separation of these proteins. Both these phenomena are implicated in cataract formation. We have used bovine gammaB crystallin as a model system to study the role of the individual cysteine residues in the aggregation and phase separation of the gamma crystallins. Here, we compare the thermodynamic and kinetic behavior of the recombinant wild-type protein (WT) and the Cys18 to Ser (C18S) mutant. We find that the solubilities of the two proteins are similar. The kinetics of crystallization, however, are different. The WT crystallizes slowly enough for the metastable liquid-liquid coexistence to be easily observed. C18S, on the other hand, crystallizes rapidly; the metastable coexisting liquid phases of the pure mutant do not form. Nevertheless, the coexistence curve of C18S can be determined provided that crystallization is kinetically suppressed. In this way we found that the coexistence curve coincides with that of the WT. Despite the difference in the kinetics of crystallization, the two proteins were found to have the same crystal forms and almost identical X-ray structures. Our results demonstrate that even conservative point mutations can bring about dramatic changes in the kinetics of crystallization. The implications of our findings for cataract formation and protein crystallization are discussed.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1I5I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5I OCA].
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</div>
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<div class="pdbe-citations 1i5i" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin., Asherie N, Pande J, Pande A, Zarutskie JA, Lomakin J, Lomakin A, Ogun O, Stern LJ, King J, Benedek GB, J Mol Biol. 2001 Dec 7;314(4):663-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11733987 11733987]
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*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Asherie, N.]]
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[[Category: Asherie N]]
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[[Category: Benedek, G B.]]
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[[Category: Benedek GB]]
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[[Category: King, J A.]]
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[[Category: King JA]]
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[[Category: Lomakin, A.]]
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[[Category: Lomakin A]]
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[[Category: Lomakin, J.]]
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[[Category: Lomakin J]]
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[[Category: Ogun, O.]]
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[[Category: Ogun O]]
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[[Category: Pande, A.]]
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[[Category: Pande A]]
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[[Category: Pande, J.]]
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[[Category: Pande J]]
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[[Category: Stern, L J.]]
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[[Category: Stern LJ]]
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[[Category: Zarutskie, J A.]]
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[[Category: Zarutskie JA]]
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[[Category: Crystallin]]
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[[Category: Eye lens protein]]
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[[Category: Structural protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:35:55 2008''
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Current revision

THE C18S MUTANT OF BOVINE (GAMMA-B)-CRYSTALLIN

PDB ID 1i5i

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