4c4r: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4r RCSB], [http://www.ebi.ac.uk/pdbsum/4c4r PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4r RCSB], [http://www.ebi.ac.uk/pdbsum/4c4r PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
beta-Phosphoglucomutase (betaPGM) catalyzes isomerization of beta-d-glucose 1-phosphate (betaG1P) into d-glucose 6-phosphate (G6P) via sequential phosphoryl transfer steps using a beta-d-glucose 1,6-bisphosphate (betaG16BP) intermediate. Synthetic fluoromethylenephosphonate and methylenephosphonate analogs of betaG1P deliver novel step 1 transition state analog (TSA) complexes for betaPGM, incorporating trifluoromagnesate and tetrafluoroaluminate surrogates of the phosphoryl group. Within an invariant protein conformation, the beta-d-glucopyranose ring in the betaG1P TSA complexes (step 1) is flipped over and shifted relative to the G6P TSA complexes (step 2). Its equatorial hydroxyl groups are hydrogen-bonded directly to the enzyme rather than indirectly via water molecules as in step 2. The (C)O-P bond orientation for binding the phosphate in the inert phosphate site differs by approximately 30 degrees between steps 1 and 2. By contrast, the orientations for the axial O-Mg-O alignment for the TSA of the phosphoryl group in the catalytic site differ by only approximately 5 degrees , and the atoms representing the five phosphorus-bonded oxygens in the two transition states (TSs) are virtually superimposable. The conformation of betaG16BP in step 1 does not fit into the same invariant active site for step 2 by simple positional interchange of the phosphates: the TS alignment is achieved by conformational change of the hexose rather than the protein. | |||
alpha-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.,Jin Y, Bhattasali D, Pellegrini E, Forget SM, Baxter NJ, Cliff MJ, Bowler MW, Jakeman DL, Blackburn GM, Waltho JP Proc Natl Acad Sci U S A. 2014 Aug 7. pii: 201402850. PMID:25104750<ref>PMID:25104750</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | |||
*[[Beta-phosphoglucomutase|Beta-phosphoglucomutase]] | |||
== References == | |||
<references/> | |||
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