4c4t: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='4c4t' size='340' side='right'caption='[[4c4t]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4c4t' size='340' side='right'caption='[[4c4t]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c4t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c4t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GRX:(S)-1-BETA-PHOSPHONOFLUOROMETHYLENE-1-DEOXY-D-GLUCOPYRANOSE'>GRX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c4r|4c4r]], [[4c4s|4c4s]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4t OCA], [https://pdbe.org/4c4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4t RCSB], [https://www.ebi.ac.uk/pdbsum/4c4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4t ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4t OCA], [http://pdbe.org/4c4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4t RCSB], [http://www.ebi.ac.uk/pdbsum/4c4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref> 
[[https://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>  
<div style="background-color:#fffaf0;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c4t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-phosphoglucomutase|Beta-phosphoglucomutase]]
*[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium lactis lister 1873]]
[[Category: Lactococcus lactis]]
[[Category: Beta-phosphoglucomutase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bowler, M W]]
[[Category: Bowler MW]]
[[Category: Pellegrini, E]]
[[Category: Pellegrini E]]
[[Category: Isomerase]]
[[Category: Metal fluoride]]
[[Category: Mutase]]
[[Category: Phosphoryl transfer]]
[[Category: Transition state]]

Revision as of 20:27, 7 September 2022

Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and aluminium tetrafluorideStructure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and aluminium tetrafluoride

Structural highlights

4c4t is a 1 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PGMB_LACLA] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.[1] [2]

See Also

References

  1. ↑ Qian N, Stanley GA, Bunte A, Radstrom P. Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene. Microbiology. 1997 Mar;143 ( Pt 3):855-65. PMID:9084169
  2. ↑ Lahiri SD, Zhang G, Dai J, Dunaway-Mariano D, Allen KN. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry. 2004 Mar 16;43(10):2812-20. PMID:15005616 doi:10.1021/bi0356810

4c4t, resolution 1.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4c4t&oldid=3619723"