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1o03

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Revision as of 09:47, 1 November 2017

Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate

Structural highlights

1o03 is a 1 chain structure with sequence from "bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1lvh, 1o08
Activity:	Beta-phosphoglucomutase, with EC number 5.4.2.6
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.

The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction.,Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13. PMID:12637673^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13. PMID:12637673 doi:10.1126/science.1082710

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o03"

@@ Line 1: / Line 1: @@
 ==Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate==
 <StructureSection load='1o03' size='340' side='right' caption='[[1o03]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lvh|1lvh]], [[1o08|1o08]]</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=1o03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o03 OCA], [http://pdbe.org/1o03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o03 RCSB], [http://www.ebi.ac.uk/pdbsum/1o03 PDBsum]</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=1o03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o03 OCA], [http://pdbe.org/1o03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o03 RCSB], [http://www.ebi.ac.uk/pdbsum/1o03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o03 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o03 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1o03" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Beta-phosphoglucomutase|Beta-phosphoglucomutase]]
 == References ==
 <references/>

1o03

From Proteopedia

Revision as of 09:47, 1 November 2017

Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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