1gla: Difference between revisions

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New page: left|200px<br /><applet load="1gla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gla, resolution 2.6Å" /> '''STRUCTURE OF THE REGU...
 
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[[Image:1gla.gif|left|200px]]<br /><applet load="1gla" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gla.gif|left|200px]]<br /><applet load="1gla" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gla, resolution 2.6&Aring;" />
caption="1gla, resolution 2.6&Aring;" />
'''STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE'''<br />
'''STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1GLA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GLA OCA].  
1GLA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLA OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
[[Category: Faber, H.R.]]
[[Category: Faber, H R.]]
[[Category: Hurley, J.H.]]
[[Category: Hurley, J H.]]
[[Category: Meadow, N.D.]]
[[Category: Meadow, N D.]]
[[Category: Pettigrew, D.W.]]
[[Category: Pettigrew, D W.]]
[[Category: Remington, S.J.]]
[[Category: Remington, S J.]]
[[Category: Roseman, S.]]
[[Category: Roseman, S.]]
[[Category: Worthylake, D.]]
[[Category: Worthylake, D.]]
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[[Category: phosphotransferase]]
[[Category: phosphotransferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:08:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:19 2008''

Revision as of 13:51, 21 February 2008

File:1gla.gif


1gla, resolution 2.6Å

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

OverviewOverview

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.

About this StructureAbout this Structure

1GLA is a Protein complex structure of sequences from Escherichia coli with as ligand. Active as Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Full crystallographic information is available from OCA.

ReferenceReference

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

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