1b2a: Difference between revisions

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New page: left|200px<br /><applet load="1b2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b2a, resolution 1.70Å" /> '''PH AFFECTS GLU B13 S...
 
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[[Image:1b2a.gif|left|200px]]<br /><applet load="1b2a" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1b2a.gif|left|200px]]<br /><applet load="1b2a" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1b2a, resolution 1.70&Aring;" />
caption="1b2a, resolution 1.70&Aring;" />
'''PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.00 COORDINATES)'''<br />
'''PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.00 COORDINATES)'''<br />


==Overview==
==Overview==
Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH, 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been, determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single, conformation at pH &lt;/= 5.80, two conformations between pH 6.00 and 6.98, and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the, conformation of GluB13 switches from one rotamer to another rotamer., Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational, change. By pH 9.00 many residues have undergone relatively large shifts, and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH, 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the, observed and calculated structure factors and map correlation coefficients, indicate that the porcine insulin structure changes gradually as a, function of pH.
Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single conformation at pH &lt;/= 5.80, two conformations between pH 6.00 and 6.98 and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the conformation of GluB13 switches from one rotamer to another rotamer. Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational change. By pH 9.00 many residues have undergone relatively large shifts and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the observed and calculated structure factors and map correlation coefficients indicate that the porcine insulin structure changes gradually as a function of pH.


==About this Structure==
==About this Structure==
1B2A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B2A OCA].  
1B2A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B2A OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Caspar, D.L.D.]]
[[Category: Caspar, D L.D.]]
[[Category: Diao, J.S.]]
[[Category: Diao, J S.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: hormone]]
[[Category: hormone]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:17:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:42 2008''

Revision as of 12:50, 21 February 2008

File:1b2a.gif


1b2a, resolution 1.70Å

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PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 6.00 COORDINATES)

OverviewOverview

Structures of porcine insulin crystals soaked in 1 M sodium sulfate at pH 5.00, 5.53, 5.80, 6.00, 6.16, 6.26, 6.35, 6.50, 6.98 and 9.00 have been determined at between 1.7 and 1.9 A resolution. GluB13 exhibits a single conformation at pH </= 5.80, two conformations between pH 6.00 and 6.98 and a single conformation at pH 9.00. Between pH 6.00 and 6.98, the conformation of GluB13 switches from one rotamer to another rotamer. Between pH 6.16 and 6.26, PheB1 undergoes a significant conformational change. By pH 9.00 many residues have undergone relatively large shifts and HisB10 exhibits a double conformation. As a result of the pH increase, the occupancy of the sulfate ion decreases from a maximum of 1.00 at pH 5.00 to a minimum of 0.46 at pH 6.50. Comparison of the structures, the observed and calculated structure factors and map correlation coefficients indicate that the porcine insulin structure changes gradually as a function of pH.

About this StructureAbout this Structure

1B2A is a Protein complex structure of sequences from Sus scrofa with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic titration of cubic insulin crystals: pH affects GluB13 switching and sulfate binding., Diao J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):670-6. Epub 2003, Mar 25. PMID:12657786

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