View source for 1up7

[[Image:1up7.jpg|left|200px]]<br /><applet load="1up7" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1up7, resolution 2.40&Aring;" />
'''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'''<br />

==Overview==
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 non-crystallographic symmetry) of the, 6-phospho-beta-glycosidase, BglT, from T.maritima in native and complexed, (NAD(+) and Glc6P) forms. Comparison of the active-center structure with, that of the 6-phospho-alpha-glucosidase GlvA from Bacillus subtilis, reveals a striking degree of structural similarity that, in light of, previous kinetic isotope effect data, allows the postulation of a common, reaction mechanism for both alpha and beta-glycosidases. Given that the, "chemistry" occurs primarily on the glycone sugar and features no, nucleophilic attack on the intact disaccharide substrate, modulation of, anomeric specificity for alpha and beta-linkages is accommodated through, comparatively minor structural changes.

==About this Structure==
1UP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with G6P, SO4 and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Endo-1,3(4)-beta-glucanase Endo-1,3(4)-beta-glucanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.6 3.2.1.6] Known structural/functional Site: <scene name='pdbsite=AC1:G6p Binding Site For Chain H'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UP7 OCA]. 

==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15670594 15670594]
[[Category: Endo-1,3(4)-beta-glucanase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Davies, G.J.]]
[[Category: Varrot, A.]]
[[Category: Withers, S.G.]]
[[Category: Yip, V.L.]]
[[Category: G6P]]
[[Category: NAD]]
[[Category: SO4]]
[[Category: 6-phospho-beta-glucosidase]]
[[Category: family4 hydrolase]]
[[Category: nad dependent]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:05:55 2007''