4ayr

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Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycinStructure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin

Structural highlights

4ayr is a 1 chain structure with sequence from Caulobacter sp. K31. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.1Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B0SWV2_CAUSK

Publication Abstract from PubMed

Mannosides in the southern hemisphere: Conformational analysis of enzymatic mannoside hydrolysis informs strategies for enzyme inhibition and inspires solutions to mannoside synthesis. Atomic resolution structures along the reaction coordinate of an inverting alpha-mannosidase show how the enzyme distorts the substrate and transition state. QM/MM calculations reveal how the free energy landscape of isolated alpha-D-mannose is molded on enzyme to only allow one conformationally accessible reaction coordinate.

The reaction coordinate of a bacterial GH47 alpha-mannosidase: a combined quantum mechanical and structural approach.,Thompson AJ, Dabin J, Iglesias-Fernandez J, Ardevol A, Dinev Z, Williams SJ, Bande O, Siriwardena A, Moreland C, Hu TC, Smith DK, Gilbert HJ, Rovira C, Davies GJ Angew Chem Int Ed Engl. 2012 Oct 29;51(44):10997-1001. doi:, 10.1002/anie.201205338. Epub 2012 Sep 26. PMID:23012075[1]

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

See Also

References

  1. Thompson AJ, Dabin J, Iglesias-Fernandez J, Ardevol A, Dinev Z, Williams SJ, Bande O, Siriwardena A, Moreland C, Hu TC, Smith DK, Gilbert HJ, Rovira C, Davies GJ. The reaction coordinate of a bacterial GH47 alpha-mannosidase: a combined quantum mechanical and structural approach. Angew Chem Int Ed Engl. 2012 Oct 29;51(44):10997-1001. doi:, 10.1002/anie.201205338. Epub 2012 Sep 26. PMID:23012075 doi:http://dx.doi.org/10.1002/anie.201205338

4ayr, resolution 1.10Å

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OCA