1abe
From Proteopedia
(New page: 200px<br /><applet load="1abe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1abe, resolution 1.7Å" /> '''NOVEL STEREOSPECIFICI...) |
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| - | [[Image:1abe.jpg|left|200px]]<br /><applet load="1abe" size=" | + | [[Image:1abe.jpg|left|200px]]<br /><applet load="1abe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1abe, resolution 1.7Å" /> | caption="1abe, resolution 1.7Å" /> | ||
'''NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN'''<br /> | '''NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tertiary structure refinement at 1.7 A resolution of the liganded form of | + | Tertiary structure refinement at 1.7 A resolution of the liganded form of L-arabinose-binding protein from Escherichia coli has revealed a novel binding site geometry which accommodates both alpha- and beta-anomers of L-arabinose. This detailed structure analysis provides new understanding of protein-sugar interaction, the process by which the binding protein minimizes the difference in the stability of the two bound sugar anomers, and the roles of periplasmic binding proteins in active transport. |
==About this Structure== | ==About this Structure== | ||
| - | 1ABE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure | + | 1ABE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1ABP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Quiocho, F | + | [[Category: Quiocho, F A.]] |
| - | [[Category: Vyas, N | + | [[Category: Vyas, N K.]] |
[[Category: binding protein]] | [[Category: binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:04 2008'' |
Revision as of 09:43, 21 February 2008
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NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN
Overview
Tertiary structure refinement at 1.7 A resolution of the liganded form of L-arabinose-binding protein from Escherichia coli has revealed a novel binding site geometry which accommodates both alpha- and beta-anomers of L-arabinose. This detailed structure analysis provides new understanding of protein-sugar interaction, the process by which the binding protein minimizes the difference in the stability of the two bound sugar anomers, and the roles of periplasmic binding proteins in active transport.
About this Structure
1ABE is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1ABP. Full crystallographic information is available from OCA.
Reference
Novel stereospecificity of the L-arabinose-binding protein., Quiocho FA, Vyas NK, Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466
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