1up7
STRUCTURE OF THE 6-PHOSPHO-BETA GLUCOSIDASE FROM THERMOTOGA MARITIMA AT 2.4 ANSTROM RESOLUTION IN THE TETRAGONAL FORM WITH NAD AND GLUCOSE-6-PHOSPHATE
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OverviewOverview
The import of disaccharides by many bacteria is achieved through their, simultaneous translocation and phosphorylation by the, phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). The, imported phospho-disaccharides are, in some cases, subsequently hydrolyzed, by members of the unusual glycoside hydrolase family GH4. The GH4 enzymes, occasionally found also in bacteria such as Thermotoga maritima that do, not utilise a PEP-PTS system, require both NAD(+) and Mn(2+) for, catalysis. A further curiosity of this family is that closely related, enzymes may show specificity for either alpha-d- or beta-d-glycosides., Here, we present, for the first time, the three-dimensional structure, (using single-wavelength anomalous dispersion methods, harnessing, extensive ... [(full description)]
About this StructureAbout this Structure
1UP7 is a [Single protein] structure of sequence from [Thermotoga maritima] with G6P, SO4 and NAD as [ligands]. Active as [Endo-1,3(4)-beta-glucanase], with EC number [3.2.1.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides., Varrot A, Yip VL, Li Y, Rajan SS, Yang X, Anderson WF, Thompson J, Withers SG, Davies GJ, J Mol Biol. 2005 Feb 18;346(2):423-35. Epub 2005 Jan 7. PMID:15670594
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