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2.4.1.83: dolichyl-phosphate beta-D-mannosyltransferase

This is an abbreviated version!
For detailed information about dolichyl-phosphate beta-D-mannosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.83

Reaction

GDP-alpha-D-mannose
+
dolichyl phosphate
=
GDP
 +
dolichyl beta-D-mannosyl phosphate

Synonyms

AglD, bDPM1, D-P-M, Dol-P Man synthase, Dol-P-Man synthase, Dol-P-Man synthase1, Dol-P-Man-synthase, Dol-P-Mansynthase, Dol-PMan synthase, dolichol phosphate mannose synthase, dolichol phosphoryl mannose synthase, dolichol-P-mannose synthase, dolicholphosphate mannose synthase, dolichyl mannosyl phosphate synthase, dolichyl phosphate mannosyltransferase, dolichyl-phosphate mannose synthase, dolichyl-phosphate mannosyltransferase, dolichyl-phospho-mannose synthase, dolichylphosphate mannose synthase, DPM, DPM synthase, DPM1, DPMS, DPMS1, GDP-Man:DolP mannosyltransferase, GDP-mannose-dolichol phosphate mannosyltransferase, GDPMan:DolP mannosyltransferase, GDPmannose-dolichylmonophosphate mannosyltransferase, GDPmannose:dolichyl-phosphate mannosyltransferase, mannosylphospho dolichol synthase, mannosylphosphodolichol synthase, mannosylphosphoryldolichol synthase, mannosyltransferase, guanosine diphosphomannose-dolichol phosphate, MPD synthase, PF0058, Pfdpm1, PfDPMS, PH0051

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.83 dolichyl-phosphate beta-D-mannosyltransferase

Crystallization

Crystallization on EC 2.4.1.83 - dolichyl-phosphate beta-D-mannosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified PfDPMS with bound GDP-Man and Mn2+ and with bound GDP and Mg2+, and acceptor substrate Dol55-P, sitting drop vapor diffusion method, 15-20 mg/ml protein is mixed with 5 mM MgCl2 or MnCl2 and either 5 mM GDP or GDP-Man in 50 mM HEPES, pH 7.5, 150 mM NaCl, 10% v/v glycerol, and 0.05% LDAO, the protein solution is mixed with crystallization solution containing 0.2 M potassium chloride, 0.1 M trisodium citrate, pH 5.5, and 37% v/v pentaerythritol propoxylate, 4°C, X-ray crystal structure determination and analysis, Dol55-P-Man structure modeling
structures of DPMS, in complex with nucleotide Mg2+, donor GDP-mannose, and glycolipid product. Substrate binding and product release are orchestrated by an interplay between juxtamembrane interface helices, donor, metal ion and acceptor. Displacement and conformational changes of the juxtamembrane interface helices, most pronouncedly of IFH2, enable entry of the dolichol-phosphate acceptor between IFH1 and IFH2, and docking of its phosphate group at Ser135 (assisted by Arg117 and Arg131), which is located immediately below the mannosyl to be transferred. The acceptor-induced changes in the juxtamembrane interface helices lead to disruption of the A-loop interaction network at the DXD motif and dislodgement of the A-loop. Collapse of the interaction network and opening of the A-loop coincides with concomitant loss of metal ion and attack by the pre-activated nucleophilic dolichol phosphate oxygen on the mannosyl C1 atom