1ave
From Proteopedia
(New page: 200px<br /><applet load="1ave" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ave, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ave.gif|left|200px]]<br /><applet load="1ave" size=" | + | [[Image:1ave.gif|left|200px]]<br /><applet load="1ave" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ave, resolution 2.8Å" /> | caption="1ave, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES'''<br /> | '''CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of hen egg-white apo-avidin, crystallized | + | The three-dimensional structure of hen egg-white apo-avidin, crystallized in a tetragonal crystal form, has been refined to a crystallographic R-factor of 0.164 (for the 6390 observed reflections in the 10.0 to 2.8 A resolution range). As in the case of holo-avidin, from which starting atomic co-ordinates were derived, the functional tetramer shows 2-pseudo 22 molecular symmetry. Each promoter is organized in an eight-stranded antiparallel orthogonal beta-barrel, with extended loop regions, which define the biotin binding pocket in the protomer core. In the absence of biotin the binding site is only partly occupied by water molecules. The structure of the binding site residues, as observed in apo-avidin, is highly complementary to that of the incoming biotin molecule, accounting for prompt and specific recognition. A crystal lattice contact may play a role in stabilizing the conformation of one protein loop, part of the biotin-binding pocket. |
==About this Structure== | ==About this Structure== | ||
| - | 1AVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1AVE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: biotin-binding protein]] | [[Category: biotin-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:41 2008'' |
Revision as of 09:48, 21 February 2008
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CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES
Overview
The three-dimensional structure of hen egg-white apo-avidin, crystallized in a tetragonal crystal form, has been refined to a crystallographic R-factor of 0.164 (for the 6390 observed reflections in the 10.0 to 2.8 A resolution range). As in the case of holo-avidin, from which starting atomic co-ordinates were derived, the functional tetramer shows 2-pseudo 22 molecular symmetry. Each promoter is organized in an eight-stranded antiparallel orthogonal beta-barrel, with extended loop regions, which define the biotin binding pocket in the protomer core. In the absence of biotin the binding site is only partly occupied by water molecules. The structure of the binding site residues, as observed in apo-avidin, is highly complementary to that of the incoming biotin molecule, accounting for prompt and specific recognition. A crystal lattice contact may play a role in stabilizing the conformation of one protein loop, part of the biotin-binding pocket.
About this Structure
1AVE is a Single protein structure of sequence from Gallus gallus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of apo-avidin from hen egg-white., Pugliese L, Malcovati M, Coda A, Bolognesi M, J Mol Biol. 1994 Jan 7;235(1):42-6. PMID:8289264
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