1b8e

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(New page: 200px<br /><applet load="1b8e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8e, resolution 1.95&Aring;" /> '''HIGH RESOLUTION CRYS...)
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[[Image:1b8e.gif|left|200px]]<br /><applet load="1b8e" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b8e, resolution 1.95&Aring;" />
caption="1b8e, resolution 1.95&Aring;" />
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP'''<br />
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP'''<br />
==Overview==
==Overview==
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The crystal structures of beta-lactoglobulin genetic variants A and B have, been determined in the orthorhombic space group C222(1) (lattice Y) by, X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The, structural comparison shows that both variants exhibit the open, conformation of the EF loop at the pH of crystallization (pH 7.9), in, contrast to what has been reported for the same genetic variants at pH 7.1, in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. &amp; Jameson, G.B. (1999) Protein Sci. 8, 75-83]., Furthermore, it was found that the stereochemical environment of Tyr42, changes significantly with pH variation between pH 7 and pH 8. This may, provide a structural explanation for an as yet unexplained feature of the, Tanford transition, namely the increase in exposure of a tyrosine residue.
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The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit the open conformation of the EF loop at the pH of crystallization (pH 7.9), in contrast to what has been reported for the same genetic variants at pH 7.1 in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. &amp; Jameson, G.B. (1999) Protein Sci. 8, 75-83]. Furthermore, it was found that the stereochemical environment of Tyr42 changes significantly with pH variation between pH 7 and pH 8. This may provide a structural explanation for an as yet unexplained feature of the Tanford transition, namely the increase in exposure of a tyrosine residue.
==About this Structure==
==About this Structure==
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1B8E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B8E OCA].
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1B8E is a [http://en.wikipedia.org/wiki/Single_protein 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=1B8E OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Oliveira, K.M.G.]]
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[[Category: Oliveira, K M.G.]]
[[Category: Polikarpov, I.]]
[[Category: Polikarpov, I.]]
[[Category: Sawyer, L.]]
[[Category: Sawyer, L.]]
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[[Category: variants]]
[[Category: variants]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:26:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:39 2008''

Revision as of 09:52, 21 February 2008


1b8e, resolution 1.95Å

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HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP

Overview

The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit the open conformation of the EF loop at the pH of crystallization (pH 7.9), in contrast to what has been reported for the same genetic variants at pH 7.1 in the trigonal space group P3221 (lattice Z) [Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. & Jameson, G.B. (1999) Protein Sci. 8, 75-83]. Furthermore, it was found that the stereochemical environment of Tyr42 changes significantly with pH variation between pH 7 and pH 8. This may provide a structural explanation for an as yet unexplained feature of the Tanford transition, namely the increase in exposure of a tyrosine residue.

About this Structure

1B8E is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition., Oliveira KM, Valente-Mesquita VL, Botelho MM, Sawyer L, Ferreira ST, Polikarpov I, Eur J Biochem. 2001 Jan;268(2):477-83. PMID:11168385

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