1abe

From Proteopedia

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-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1abe ConSurf].
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Revision as of 02:27, 10 February 2016

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

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1abe, resolution 1.70Å

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1abe is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1abp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ARAF_ECOLI] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Novel stereospecificity of the L-arabinose-binding protein.,Quiocho FA, Vyas NK Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Quiocho FA, Vyas NK. Novel stereospecificity of the L-arabinose-binding protein. Nature. 1984 Aug 2-8;310(5976):381-6. PMID:6379466

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

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Categories: Bacillus coli migula 1895 | Quiocho, F A | Vyas, N K | Binding protein

1abe

From Proteopedia

Revision as of 02:27, 10 February 2016

NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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