1glb

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(Difference between revisions)

Revision as of 06:35, 29 November 2017

STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE

Structural highlights

1glb is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PTGA_ECOLI] The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. [GLPK_ECOLI] Key enzyme in the regulation of glycerol uptake and metabolism.[HAMAP-Rule:MF_00186]

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

The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS carbohydrate transport systems by binding to diverse target proteins. The crystal structure at 2.6 A resolution of one of the targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined. GK contains a region that is topologically identical to the adenosine triphosphate binding domains of hexokinase, the 70-kD heat shock cognate, and actin. IIIGlc binds far from the catalytic site of GK, indicating that long-range conformational changes mediate the inhibition of GK by IIIGlc. GK and IIIGlc are bound by hydrophobic and electrostatic interactions, with only one hydrogen bond involving an uncharged group. The phosphorylation site of IIIGlc, His90, is buried in a hydrophobic environment formed by the active site region of IIIGlc and a 3(10) helix of GK, suggesting that phosphorylation prevents IIIGlc binding to GK by directly disrupting protein-protein interactions.

Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase.,Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ Science. 1993 Jan 29;259(5095):673-7. PMID:8430315^[1]

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

References

↑ Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ. Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science. 1993 Jan 29;259(5095):673-7. PMID:8430315

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/1glb"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE==
 <StructureSection load='1glb' size='340' side='right' caption='[[1glb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </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=1glb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glb OCA], [http://pdbe.org/1glb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glb RCSB], [http://www.ebi.ac.uk/pdbsum/1glb 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=1glb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glb OCA], [http://pdbe.org/1glb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1glb RCSB], [http://www.ebi.ac.uk/pdbsum/1glb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1glb ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1glb" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Glycerol kinase|Glycerol kinase]]
 == References ==
 <references/>

1glb

From Proteopedia

Revision as of 06:35, 29 November 2017

STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

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