1aqb

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(New page: 200px<br /><applet load="1aqb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aqb, resolution 1.65&Aring;" /> '''RETINOL-BINDING PROT...)
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[[Image:1aqb.gif|left|200px]]<br /><applet load="1aqb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1aqb, resolution 1.65&Aring;" />
caption="1aqb, resolution 1.65&Aring;" />
'''RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA'''<br />
'''RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA'''<br />
==Overview==
==Overview==
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The crystal structure of pig plasma retinol-binding protein (RBP) has been, determined at 1.65 A resolution. The space group is P212121, with a =, 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the, asymmetric unit. The structure has been solved using the molecular, replacement method and refined with restrained least squares to an R, factor of 0.1844 and an Rfree of 0.237 for 18 874 and 1001 independent, reflections, respectively. The relatively high resolution structure of pig, holoRBP has revealed some new structural details. Moreover, it has, provided a description of the binding site for Cd2+, a metal ion which is, required for protein crystallization. The hepta-coordination of the, RBP-bound cadmium ion involves different residues of two symmetry-related, RBP molecules, consistent with the participation of the cation in, intermolecular interactions that in turn promote protein crystallization.
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The crystal structure of pig plasma retinol-binding protein (RBP) has been determined at 1.65 A resolution. The space group is P212121, with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R factor of 0.1844 and an Rfree of 0.237 for 18 874 and 1001 independent reflections, respectively. The relatively high resolution structure of pig holoRBP has revealed some new structural details. Moreover, it has provided a description of the binding site for Cd2+, a metal ion which is required for protein crystallization. The hepta-coordination of the RBP-bound cadmium ion involves different residues of two symmetry-related RBP molecules, consistent with the participation of the cation in intermolecular interactions that in turn promote protein crystallization.
==About this Structure==
==About this Structure==
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1AQB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa_domestica Sus scrofa domestica] with CD and RTL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AQB OCA].
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1AQB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa_domestica Sus scrofa domestica] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=RTL:'>RTL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQB OCA].
==Reference==
==Reference==
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[[Category: vitamin a]]
[[Category: vitamin a]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:02:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:22 2008''

Revision as of 09:47, 21 February 2008


1aqb, resolution 1.65Å

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RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA

Overview

The crystal structure of pig plasma retinol-binding protein (RBP) has been determined at 1.65 A resolution. The space group is P212121, with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R factor of 0.1844 and an Rfree of 0.237 for 18 874 and 1001 independent reflections, respectively. The relatively high resolution structure of pig holoRBP has revealed some new structural details. Moreover, it has provided a description of the binding site for Cd2+, a metal ion which is required for protein crystallization. The hepta-coordination of the RBP-bound cadmium ion involves different residues of two symmetry-related RBP molecules, consistent with the participation of the cation in intermolecular interactions that in turn promote protein crystallization.

About this Structure

1AQB is a Single protein structure of sequence from Sus scrofa domestica with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of pig plasma retinol-binding protein at 1.65 A resolution., Zanotti G, Panzalorto M, Marcato A, Malpeli G, Folli C, Berni R, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1049-52. PMID:9757135

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